{"id":403,"date":"2015-09-01T18:16:47","date_gmt":"2015-09-01T18:16:47","guid":{"rendered":"https:\/\/carolpostgroup.wordpress.com\/?page_id=11"},"modified":"2021-01-15T04:13:20","modified_gmt":"2021-01-15T04:13:20","slug":"publications","status":"publish","type":"page","link":"https:\/\/www.purdue.edu\/postlab\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"<div style=\"font-family: verdana;font-size: 90%;color: black\">\n<ul>\n<li>Wu, H, Huang, H &amp; Post, CB. (2020) All-atom adaptively biased path optimization of Src kinase conformational inactivation: Switched electrostatic network in the concerted motion of \u03b1C helix and the activation loop.&nbsp;<i>The Journal of Chemical Physics<\/i>&nbsp;<b>153:<\/b> 175101. [<a href=\"https:\/\/doi.org\/10.1063\/5.0021603\" target=\"_blank\" rel=\"noopener noreferrer\">doi<\/a>] [<a href=\"\/postlab\/wp-content\/uploads\/2021\/01\/2020.JCP_.Wu_.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">pdf<\/a>].<\/li>\n<li>Joshi MK, Burton RA, Wu H, Lipchik AM, Craddock BP, Mo H, Parker LL, Miller WT, Post CB (2019) Substrate binding to Src: a new perspective on tyrosine kinase substrate recognition from NMR and molecular dynamics. <em>Protein Science<\/em>. [<a href=\"https:\/\/onlinelibrary.wiley.com\/doi\/abs\/10.1002\/pro.3777\" target=\"_blank\" rel=\"noopener noreferrer\">doi<\/a>]<\/li>\n<li>Feng C, Kovrigin EL, Post CB (2019) NmrLineGuru: Standalone and User-Friendly GUIs for Fast 1D NMR Lineshape Simulation and Analysis of Multi-State Equilibrium Binding Models. <em>Scientific Reports<\/em> 9:16023. [<a href=\"https:\/\/doi.org\/10.1038\/s41598-019-52451-8\" target=\"_blank\" rel=\"noopener noreferrer\">doi<\/a>]<\/li>\n<li>Krabill AD, Chen H, Hussain S, Feng C, Abdullah A, Das C, Aryal K, Post CB, Wendt MK, Galardy PJ, et al. (2019) Ubiquitin C-Terminal Hydrolase L1: Biochemical and Cellular Characterization of a Covalent Cyanopyrrolidine-Based Inhibitor. <em>Chembiochem<\/em>. [<a href=\"https:\/\/doi.org\/10.1002\/cbic.201900434\" target=\"_blank\" rel=\"noopener noreferrer\">doi<\/a>]<\/li>\n<li>Kim D, Sun Y, Xie D, Denton KE, Chen H, Lin H, Wendt MK, Post CB, Krusemark CJ (2019) Application of a Substrate-Mediated Selection with c-Src Tyrosine Kinase to a DNA-Encoded Chemical Library. <em>Molecules<\/em> 24:2764. [<a href=\"https:\/\/doi.org\/10.3390\/molecules24152764\" target=\"_blank\" rel=\"noopener noreferrer\">doi<\/a>]<\/li>\n<li>Wu H, Post CB (2018) Protein Conformational Transitions from All-Atom Adaptively Biased Path Optimization.<cite>J. Chem. Theory Comput.<\/cite> <strong>14<\/strong>:5372\u20135382. [<a href=\"http:\/\/dx.doi.org\/10.1021\/acs.jctc.8b00147\" target=\"_blank\" rel=\"noopener noreferrer\">doi<\/a>]&nbsp;[<a href=\"\/postlab\/wp-content\/uploads\/2018\/11\/2018JCTCWu.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">pdf<\/a>]<\/li>\n<li>Feng C, Roy A, Post CB (2018) Entropic allostery dominates the phosphorylation-dependent regulation of Syk tyrosine kinase release from immunoreceptor tyrosine-based activation motifs: Entropic Allostery Dominates Syk Release. <em>Protein Science<\/em> <strong>27<\/strong>:1780\u20131796.&nbsp;[<a href=\"http:\/\/dx.doi.org\/10.1002\/pro.3489\" target=\"_blank\" rel=\"noopener noreferrer\">doi<\/a>]&nbsp;[<a href=\"\/postlab\/wp-content\/uploads\/2018\/11\/2018ProSciFeng.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">pdf<\/a>]<\/li>\n<li>Post, CB &amp; Levy, RM. (2017) Editorial overview: Theory &amp; computation.&nbsp;<i>Curr. Opin. Struct. Biol.<\/i>&nbsp;<b>43:<\/b> iv-vi. pmcid: PMC6225781.&nbsp;[<a href=\"https:\/\/doi.org\/10.1016\/j.sbi.2017.04.008\" target=\"_blank\" rel=\"noopener noreferrer\">doi<\/a>]<\/li>\n<li>Mo, H, Harwood, JS, Yang, D &amp; Post, CB. (2017) A simple method for NMR&nbsp;<em>t<\/em><sub>1<\/sub> noise suppression.&nbsp;<em>J. Magn. Res.&nbsp;<\/em><strong>276: <\/strong>43-50. <a href=\"http:\/\/dx.doi.org\/10.1016\/j.jmr.2016.12.014\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a>&nbsp; &nbsp;&nbsp;<\/li>\n<li>Skeel, RD, Zhao, R &amp; Post, CB. (2017) A minimization principle for transitions paths of maximum flux for collective variables.&nbsp;<em>Theor. Chem. Accts.<\/em>&nbsp;<strong>136:<\/strong> 1-14.&nbsp;<a href=\"http:\/\/doi.org\/10.1007\/s00214-016-2041-3\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a><\/li>\n<li>Roy, A, Hua, DP &amp; Post, CB. (2016) Analysis of multi-domain protein dynamics.&nbsp;<cite>J. Chem. Theory Comput.<\/cite>&nbsp;<strong><span class=\"citation_volume\">12:<\/span><\/strong>&nbsp;274\u2013280. <a href=\"http:\/\/doi.org\/10.1021\/acs.jctc.5b00796\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a>&nbsp;<a href=\"\/postlab\/wp-content\/uploads\/Publications\/2016JCTCRoy.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Feng, C &amp; Post, CB. (2016) Insights into the allosteric regulation of Syk association with receptor ITAM, a multi-state equilibrium.&nbsp;<i>Phys. Chem. Chem. Phys.<\/i>&nbsp;<strong>18:&nbsp;<\/strong>5807-5818. <a href=\"http:\/\/doi.org\/10.1039\/c5cp05417f\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a>&nbsp;<a href=\"\/postlab\/wp-content\/uploads\/Publications\/2016PCCPFeng-wSI.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Hua, DP, Huang, H, Roy, A &amp; Post, CB. (2016) Evaluating the dynamics and electrostatic interactions of folded proteins in implicit solvents. <em>Protein Science<\/em> <strong>25:<\/strong> 204-218.&nbsp;<a href=\"http:\/\/doi.org\/10.1002\/pro.2753\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2016ProSciHua-wSI.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Dickson, B, Feng, C, Huang, H, Joshi, M &amp; Post, CB. (2015) Expanding the conformational space of structure\/function relationship of tyrosine kinases.&nbsp;<i>J Biomol Struct Dyn<\/i>&nbsp;<b>33 Suppl 1:<\/b> 29. [<a href=\"https:\/\/doi.org\/10.1080\/07391102.2015.1032591\" target=\"_blank\" rel=\"noopener noreferrer\">doi<\/a>]<\/li>\n<li>Ysselstein, D, Joshi, M, Mishra, V, Griggs, AM, Asiago, JM, McCabe, GP, Stanciu, LA, Post, CB &amp; Rochet, J-C. (2015) Effects of impaired membrane interactions on \u03b1-synuclein aggregation and neurotoxicity. <i>Neurobiology of Disease<\/i> <b>79:<\/b> 150-163.&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1016\/j.nbd.2015.04.007\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2015NeurbioDisRochet.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Kuhn, RJ, Dowd, KA, Beth Post, C &amp; Pierson, TC. (2015) Shake, rattle, and roll: Impact of the dynamics of flavivirus particles on their interactions with the host. <i>Virology<\/i> <b>479\u2013480:<\/b> 508-517. doi: 10.1016\/j.virol.2015.03.025.&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1016\/j.virol.2015.03.025\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2015VirologyPierson.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Roy, A, Hua, DP, Ward, JM &amp; Post, CB. (2014) Relative Binding Enthalpies from Molecular Dynamics Simulations Using a Direct Method. <i>Journal of Chemical Theory and Computation (Special Issue on Free Energy)<\/i> <b>10:<\/b> 2759-2768.&nbsp;<a href=\"http:\/\/doi.org\/10.1021\/ct500200n\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2014JCTCRoyHuaWard-wSI.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Yu, S, Huang, H, Iliuk, A, Wang, W-H, Jayasundera, KB, Tao, WA, Post, CB &amp; Geahlen, RL. (2013) Syk Inhibits the Activity of Protein Kinase A by Phosphorylating Tyrosine 330 of the Catalytic Subunit. <i>Journal of Biological Chemistry<\/i> <b>288:<\/b> 10870-10881.&nbsp;<a href=\"http:\/\/doi.org\/10.1074\/jbc.M112.426130\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2013JBCYu.Geahlen.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Chen, C-H, Piraner, D, Gorenstein, NM, Geahlen, RL &amp; Beth Post, C. (2013) Differential recognition of syk-binding sites by each of the two phosphotyrosine-binding pockets of the Vav SH2 domain. <i>Biopolymers 50th Anniversary Special Issue<\/i> <b>99:<\/b> 897-907.&nbsp;<a href=\"http:\/\/doi.org\/10.1002\/bip.22371\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2013BiopolymersChen.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Roy, A &amp; Post, CB. (2012) Long-distance correlations of rhinovirus capsid dynamics contribute to uncoating and antiviral activity. <i>Proc Natl Acad Sci U S A<\/i> <b>109:<\/b> 5271-5276.&nbsp;<a href=\"http:\/\/doi.org\/10.1073\/pnas.1119174109\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2012PNASRoy-wSI.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Roy, A &amp; Post, CB. (2012) Detection of Long-Range Concerted Motions in Protein by a Distance Covariance. <i>Journal of Chemical Theory and Computation<\/i> <b>8:<\/b> 3009-3014.&nbsp;<a href=\"http:\/\/doi.org\/10.1021\/ct300565f\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2012JCTCRoy-wSI.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Huang, H, Zhao, R, Dickson, BM, Skeel, RD &amp; Post, CB. (2012) \u03b1C helix as a switch in the conformational transition of Src\/CDK-like kinase domains. <i>J Phys Chem B<\/i> <b>116:<\/b> 4465-4475.&nbsp;<a href=\"http:\/\/doi.org\/10.1021\/jp301628r\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2012JPCHuang_wSI.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Dickson, BM, Huang, H &amp; Post, CB. (2012) Unrestrained Computation of Free Energy along a Path. <i>J Phys Chem B<\/i> <b>116:<\/b> 11046-11055.&nbsp;<a href=\"http:\/\/doi.org\/10.1021\/jp304720m\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2012JPCDickson.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Dadarlat, VM, Gorenstein, LA &amp; Post, CB. (2012) Prediction of protein relative enthalpic stability from molecular dynamics simulations of the folded and unfolded States. <i>Biophys J<\/i> <b>103:<\/b> 1762-1773.&nbsp;<a href=\"http:\/\/doi.org\/10.1016\/j.bpj.2012.08.048\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2012BJDadarlat.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Yuwen, T, Post, CB &amp; Skrynnikov, NR. (2011) Domain cooperativity in multidomain proteins: what can we learn from molecular alignment in anisotropic media? <i>J Biomol NMR<\/i> <b>51:<\/b> 131-150.&nbsp;<a href=\"http:\/\/doi.org\/10.1007\/s10858-011-9548-7\" target=\"_blank\" rel=\"noopener noreferrer\">[doi] <\/a><a href=\"http:\/\/2011JBioNMRSSkrynnikov\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Roy, A &amp; Post, CB. (2011) Microscopic Symmetry Imposed by Rotational Symmetry Boundary Conditions in Molecular Dynamics Simulation. <i>J Chem Theory Comput<\/i> <b>7:<\/b> 3346-3353.&nbsp;<a href=\"http:\/\/doi.org\/10.1021\/ct2000843\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2011JCTCRoy-RBC-wSI.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Lundgaard, GL, Daniels, NE, Pyndiah, S, Cassimere, EK, Ahmed, KM, Rodrigue, A, Kihara, D, Post, CB &amp; Sakamuro, D. (2011) Identification of a novel effector domain of BIN1 for cancer suppression. <i>J Cell Biochem<\/i> <b>112:<\/b> 2992-3001.&nbsp;<a href=\"http:\/\/doi.org\/10.1002\/jcb.23222\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2011JCBLundgaard.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Chen, CH, Martin, VA, Gorenstein, NM, Geahlen, RL &amp; Post, CB. (2011) Two closely spaced tyrosines regulate NFAT signaling in B cells via Syk association with Vav. <i>Mol Cell Biol<\/i> <b>31:<\/b> 2984-2996.&nbsp;<a href=\"http:\/\/doi.org\/10.1128\/MCB.05043-11\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2011MCBChen.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Ward, JM, Gorenstein, NM, Tian, J, Martin, SF &amp; Post, CB. (2010) Constraining binding hot spots: NMR and molecular dynamics simulations provide a structural explanation for enthalpy-entropy compensation in SH2-ligand binding. <i>J Am Chem Soc<\/i> <b>132:<\/b> 11058-11070.&nbsp;<a href=\"http:\/\/doi.org\/10.1021\/ja910535j\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2010JACSWard-wSI.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Taylor, GM, Ma, L, Vogt, VM &amp; Post, CB. (2010) NMR relaxation studies of an RNA-binding segment of the rous sarcoma virus gag polyprotein in free and bound states: a model for autoinhibition of assembly. <i>Biochemistry<\/i> <b>49:<\/b> 4006-4017.&nbsp;<a href=\"http:\/\/doi.org\/10.1021\/bi902196e\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2010TaylorBiochem-wSI.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Kularatne, SA, Zhou, Z, Yang, J, Post, CB &amp; Low, PS. (2009) Design, synthesis, and preclinical evaluation of prostate-specific membrane antigen targeted (99m)Tc-radioimaging agents. <i>Mol Pharm<\/i> <b>6:<\/b> 790-800.&nbsp;<a href=\"http:\/\/doi.org\/10.1021\/mp9000712\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2009MolPharmKularatne.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Huang, H, Ozkirimli, E &amp; Post, CB. (2009) A Comparison of Three Perturbation Molecular Dynamics Methods for Modeling Conformational Transitions. <i>J Chem Theory Comput<\/i> <b>5:<\/b> 1301-1314.&nbsp;<a href=\"http:\/\/doi.org\/10.1021\/ct9000153\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2009JCTCHuang.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Brooks, BR, Brooks, CL, 3rd, Mackerell, AD, Jr., Nilsson, L, Petrella, RJ, Roux, B, Won, Y, Archontis, G, Bartels, C, Boresch, S, Caflisch, A, Caves, L, Cui, Q, Dinner, AR, Feig, M, Fischer, S, Gao, J, Hodoscek, M, Im, W, Kuczera, K, Lazaridis, T, Ma, J, Ovchinnikov, V, Paci, E, Pastor, RW, Post, CB, Pu, JZ, Schaefer, M, Tidor, B, Venable, RM, Woodcock, HL, Wu, X, Yang, W, York, DM &amp; Karplus, M. (2009) CHARMM: the biomolecular simulation program. <i>J Comput Chem<\/i> <b>30:<\/b> 1545-1614.&nbsp;<a href=\"http:\/\/doi.org\/10.1002\/jcc.21287\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2009JCC-CHARMM.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Zhou, Z, Khaliq, M, Suk, JE, Patkar, C, Li, L, Kuhn, RJ &amp; Post, CB. (2008) Antiviral compounds discovered by virtual screening of small-molecule libraries against dengue virus E protein. <i>ACS Chem Biol<\/i> <b>3:<\/b> 765-775.&nbsp;<a href=\"http:\/\/doi.org\/10.1021\/cb800176t\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2008ACSChemBiolZhou-wSI.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Zhang, Y, Oh, H, Burton, RA, Burgner, JW, Geahlen, RL &amp; Post, CB. (2008) Tyr130 phosphorylation triggers Syk release from antigen receptor by long-distance conformational uncoupling. <i>Proc Natl Acad Sci U S A<\/i> <b>105:<\/b> 11760-11765.&nbsp;<a href=\"http:\/\/doi.org\/10.1073\/pnas.0708583105\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2008PNASZhang-wSI.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Ozkirimli, E, Yadav, SS, Miller, WT &amp; Post, CB. (2008) An electrostatic network and long-range regulation of Src kinases. <i>Protein Sci (accelerated article)<\/i> <b>17:<\/b> 1871-1880.&nbsp;<a href=\"http:\/\/doi.org\/10.1110\/ps.037457.108\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2008PSOzkirimli.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Li, Z, Khaliq, M, Zhou, Z, Post, CB, Kuhn, RJ &amp; Cushman, M. (2008) Design, synthesis, and biological evaluation of antiviral agents targeting flavivirus envelope proteins. <i>J Med Chem<\/i> <b>51:<\/b> 4660-4671.&nbsp;<a href=\"http:\/\/doi.org\/10.1021\/jm800412d\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2008JMCLi-eprot.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Dadarlat, VM &amp; Post, CB. (2008) Contribution of charged groups to the enthalpic stabilization of the folded states of globular proteins. <i>J Phys Chem B<\/i> <b>112:<\/b> 6159-6167. &nbsp;<a href=\"http:\/\/doi.org\/10.1021\/jp077024d\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2008JPCDadarlat.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Ozkirimli, E &amp; Post, CB. (2006) Src kinase activation: A switched electrostatic network. <i>Protein Sci<\/i> <b>15:<\/b> 1051-1062. <a href=\"http:\/\/doi.org\/10.1110\/ps.051999206\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2006PSOzkirimli.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Jao, SC, English Ospina, SM, Berdis, AJ, Starke, DW, Post, CB &amp; Mieyal, JJ. (2006) Computational and mutational analysis of human glutaredoxin (thioltransferase): probing the molecular basis of the low pKa of cysteine 22 and its role in catalysis. <i>Biochemistry<\/i> <b>45:<\/b> 4785-4796.&nbsp;<a href=\"http:\/\/doi.org\/10.1021\/bi0516327\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2006BiochmJao.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Groesch, TD, Zhou, F, Mattila, S, Geahlen, RL &amp; Post, CB. (2006) Structural basis for the requirement of two phosphotyrosine residues in signaling mediated by Syk tyrosine kinase. <i>J Mol Biol<\/i> <b>356:<\/b> 1222-1236.&nbsp;<a href=\"http:\/\/doi.org\/10.1016\/j.jmb.2005.11.095\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2006JMBGroesch-wSI.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Dadarlat, VM &amp; Post, CB. (2006) Decomposition of protein experimental compressibility into intrinsic and hydration shell contributions. <i>Biophys J<\/i> <b>91:<\/b> 4544-4554.&nbsp;<a href=\"http:\/\/doi.org\/10.1529\/biophysj.106.087726\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2006BJDadarlat.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Burton, RA, Mattila, S, Taparowsky, EJ &amp; Post, CB. (2006) B-myc: N-terminal recognition of myc binding proteins. <i>Biochemistry<\/i> <b>45:<\/b> 9857-9865. <a href=\"http:\/\/doi.org\/10.1021\/bi060379n\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2006BiochmBurton.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Wilkinson, TA, Tellinghuisen, TL, Kuhn, RJ &amp; Post, CB. (2005) Association of sindbis virus capsid protein with phospholipid membranes and the E2 glycoprotein: implications for alphavirus assembly. <i>Biochemistry<\/i> <b>44:<\/b> 2800-2810.&nbsp;<a href=\"http:\/\/doi.org\/10.1021\/bi0479961\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2005BiochemWilkinson.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Moon, KD, Post, CB, Durden, DL, Zhou, Q, De, P, Harrison, ML &amp; Geahlen, RL. (2005) Molecular basis for a direct interaction between the Syk protein-tyrosine kinase and phosphoinositide 3-kinase. <i>J Biol Chem<\/i> <b>280:<\/b> 1543-1551.&nbsp;<a href=\"http:\/\/doi.org\/10.1074\/jbc.M407805200\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2005JBCMoon.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Li, Y, Zhou, Z &amp; Post, CB. (2005) Dissociation of an antiviral compound from the internal pocket of human rhinovirus 14 capsid. <i>Proc Natl Acad Sci U S A<\/i> <b>102:<\/b> 7529-7534. <a href=\"http:\/\/doi.org\/10.1073\/pnas.0408749102\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2005PNASLi.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Ma, L, Jones, CT, Groesch, TD, Kuhn, RJ &amp; Post, CB. (2004) Solution structure of dengue virus capsid protein reveals another fold. <i>Proc Natl Acad Sci U S A<\/i> <b>101:<\/b> 3414-3419.&nbsp;<a href=\"http:\/\/doi.org\/10.1073\/pnas.0305892101\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2004PNASMa.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB. (2003) Exchange-transferred NOE spectroscopy and bound ligand structure determination. <i>Curr Opin Struct Biol<\/i> <b>13:<\/b> 581-588.&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1016\/j.sbi.2003.09.012\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2003COSBPost.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Jones, CT, Ma, L, Burgner, JW, Groesch, TD, Post, CB &amp; Kuhn, RJ. (2003) Flavivirus capsid is a dimeric alpha-helical protein. <i>J Virol<\/i> <b>77:<\/b> 7143-7149156156.&nbsp;<a href=\"http:\/\/doi.org\/10.1128\/JVI.77.12.7143-7149.2003\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2003JVirolJones.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Dadarlat, VM &amp; Post, CB. (2003) Adhesive-cohesive model for protein compressibility: an alternative perspective on stability. <i>Proc Natl Acad Sci U S A<\/i> <b>100:<\/b> 14778-14783.&nbsp;<a href=\"http:\/\/doi.org\/10.1073\/pnas.2434157100\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2003PNASDadarlat.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Zabell, AP &amp; Post, CB. (2002) Docking multiple conformations of a flexible ligand into a protein binding site using NMR restraints. <i>Proteins<\/i> <b>46:<\/b> 295-307.&nbsp;<a href=\"http:\/\/doi.org\/10.1002\/prot.10017\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2002ProteinsZabell.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Zabell, AP &amp; Post, CB. (2002) Intermolecular relaxation has little effect on intra-peptide exchange-transferred NOE intensities. <i>J Biomol NMR<\/i> <b>22:<\/b> 303-315. <a href=\"http:\/\/doi.org\/10.1023\/A:1014989407261\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2002JBNMRZabell.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB. (2002) Transition States: Substrate-induced Conformational Transitions. pp.&nbsp; In <i>Encyclopedia of Life Sciences<\/i>, Wiley. <a href=\"http:\/\/doi.org\/10.1038\/npg.els.0000604\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2002ELSPost.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Speelman, B, Brooks, BR &amp; Post, CB. (2001) Molecular dynamics simulations of human rhinovirus and an antiviral compound. <i>Biophys J<\/i> <b>80:<\/b> 121-129. <a href=\"http:\/\/dx.doi.org\/10.1016%2FS0006-3495(01)75999-1\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2001BJSpeelman.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, C &amp; Dadarlat, V. (2001) Molecular Dynamics Simulations of Biological Macromolecules. pp. 489-495 In <i>International Tables for Crystallography.&nbsp; Crystallography of Biological Macromolecules<\/i>. (eds. M. Rossmann, and E. Arnold), Kluwer Academic, London.<\/li>\n<li>Dadarlat, VM &amp; Post, CB. (2001) Insights into protein compressibility from molecular dynamics simulations. <i>Journal of Physical Chemistry B<\/i> <b>105:<\/b> 715-724.&nbsp;<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/jp0024118\" target=\"_blank\" rel=\"noopener noreferrer\">[doi] <\/a><a href=\"\/postlab\/wp-content\/uploads\/Publications\/2001JPCDadarlat-wSI.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Wilkinson, TA, Yin, J, Pidgeon, C &amp; Post, CB. (2000) Alkylation of cysteine-containing peptides to mimic palmitoylation. <i>J Pept Res<\/i> <b>55:<\/b> 140-147. <a href=\"http:\/\/doi.org\/10.1034\/j.1399-3011.2000.00164.x\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2000JPepRWilkinson.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Phelps, DK, Speelman, B &amp; Post, CB. (2000) Theoretical studies of viral capsid proteins. <i>Curr Opin Struct Biol<\/i> <b>10:<\/b> 170-173. <a href=\"http:\/\/europepmc.org\/abstract\/med\/10753813\" target=\"_blank\" rel=\"noopener noreferrer\">[doi] <\/a><a href=\"\/postlab\/wp-content\/uploads\/Publications\/2000COSBPhelps.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Kingston, RL, Fitzon-Ostendorp, T, Eisenmesser, EZ, Schatz, GW, Vogt, VM, Post, CB &amp; Rossmann, MG. (2000) Structure and self-association of the Rous sarcoma virus capsid protein. <i>Structure<\/i> <b>8:<\/b> 617-628. <a href=\"http:\/\/doi.org\/10.1016\/S0969-2126(00)00148-9\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2000StrctKingston.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Gaul, BS, Harrison, ML, Geahlen, RL, Burton, RA &amp; Post, CB. (2000) Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor. <i>J Biol Chem<\/i> <b>275:<\/b> 16174-16182. <a href=\"http:\/\/doi.org\/10.1074\/jbc.M909044199\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2000JBCGaul.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Eisenmesser, EZ, Zabell, AP &amp; Post, CB. (2000) Accuracy of bound peptide structures determined by exchange transferred nuclear Overhauser data: a simulation study. <i>J Biomol NMR<\/i> <b>17:<\/b> 17-32. <a href=\"http:\/\/link.springer.com\/article\/10.1023%2FA%3A1008311703619\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/2000JBNMREisenmesser.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB, Gaul, BS, Eisenmesser, EZ &amp; Schneider, ML. (1999) NMR structure of phospho-tyrosine signaling complexes. <i>Med Res Rev<\/i> <b>19:<\/b> 295-305.&nbsp;&lt;a href=&#8221;http:\/\/doi.org\/10.1002\/(SICI)1098-1128(199907)19:43.0.CO;2-5&#8243; target=&#8221;_blank&#8221; rel=&#8221;noopener&#8221;&gt;[doi] <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1999MRRPost.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Pomes, R, Eisenmesser, E, Post, CB &amp; Roux, B. (1999) Calculating excess chemical potentials using dynamic simulations in the fourth dimension. <i>Journal of Chemical Physics<\/i> <b>111:<\/b> 3387-3395. <a href=\"http:\/\/doi.org\/10.1063\/1.479622\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1999JCPPomes.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Phelps, DK &amp; Post, CB. (1999) Molecular dynamics investigation of the effect of an antiviral compound on human rhinovirus. <i>Protein Sci<\/i> <b>8:<\/b> 2281-2289. <a href=\"http:\/\/doi.org\/10.1110\/ps.8.11.2281\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1999PSPhelps.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Reddy, VS, Giesing, HA, Morton, RT, Kumar, A, Post, CB, Brooks, CL, 3rd &amp; Johnson, JE. (1998) Energetics of quasiequivalence: computational analysis of protein-protein interactions in icosahedral viruses. <i>Biophys J<\/i> <b>74:<\/b> 546-558.&nbsp;<a href=\"http:\/\/doi.org\/10.1016\/S0006-3495(98)77813-0\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1998BJReddy.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Phelps, DK, Rossky, PJ &amp; Post, CB. (1998) Influence of an antiviral compound on the temperature dependence of viral protein flexibility and packing: a molecular dynamics study. <i>J Mol Biol<\/i> <b>276:<\/b> 331-337.&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1006\/jmbi.1997.1542\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1998JMBPhelps.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Eisenmesser, EZ &amp; Post, CB. (1998) Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase. <i>Biochemistry<\/i> <b>37:<\/b> 867-877. <a href=\"http:\/\/doi.org\/10.1021\/bi971445b\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1998BiochemEisenmesser.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Vincent, SJ, Zwahlen, C, Post, CB, Burgner, JW &amp; Bodenhausen, G. (1997) The conformation of NAD+ bound to lactate dehydrogenase determined by nuclear magnetic resonance with suppression of spin diffusion. <i>Proc Natl Acad Sci U S A<\/i> <b>94:<\/b> 4383-438820731.&nbsp;<a href=\"http:\/\/doi.org\/10.1073\/pnas.94.9.4383\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1997PNASVincent.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Zheng, J &amp; Post, CB. (1996) Variation in protein indirect relaxation effects in one- and two-dimensional exchange-transferred Overhauser experiments. <i>Journal of Physical Chemistry<\/i> <b>100:<\/b> 2675-2680. <a href=\"http:\/\/doi.org\/10.1021\/jp952960r\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> [pdf]<\/li>\n<li>Zhang, Z, Post, CB &amp; Smith, DL. (1996) Amide hydrogen exchange determined by mass spectrometry: application to rabbit muscle aldolase. <i>Biochemistry<\/i> <b>35:<\/b> 779-791. <a href=\"http:\/\/doi.org\/10.1021\/bi952227q\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1996JPCZheng.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Young, L &amp; Post, CB. (1996) Catalysis by entropic guidance from enzymes. <i>Biochemistry (New Concepts article)<\/i> <b>35:<\/b> 15129-15133. <a href=\"http:\/\/doi.org\/10.1021\/bi961875m\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1996BiochmYoung.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB &amp; Schneider, ML. (1996) Phosphotyrosyl peptide-enzyme complexes: How much structure can we get from transferred NOE&#8217;s? In <i>NMR as a Structural Tool for Macromolecules: Current Status and Future Directions, [Proceedings of an International Symposium on NMR as a Structural Tool for Macromolecules: Current Status and Future Directions], Indianapolis, Oct. 30-Nov. 1, 1994<\/i>, pp. 91-101.&nbsp;<a href=\"http:\/\/doi.org\/10.1016\/j.pbiomolbio.2014.08.012\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> [pdf]<\/li>\n<li>Karplus, M &amp; Post, CB. (1996) <i>Simulations of lysozyme: internal motions and the reaction mechanism<\/i>, 1996\/01\/01 ed.&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/8765298\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> [pdf]<\/li>\n<li>Schneider, ML &amp; Post, CB. (1995) Solution structure of a band 3 peptide inhibitor bound to aldolase: a proposed mechanism for regulating binding by tyrosine phosphorylation. <i>Biochemistry<\/i> <b>34:<\/b> 16574-16584. <a href=\"http:\/\/doi.org\/10.1021\/bi00051a005\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> [pdf]<\/li>\n<li>Post, CB &amp; Ray, WJ, Jr. (1995) Reexamination of induced fit as a determinant of substrate specificity in enzymatic reactions. <i>Biochemistry (New Concepts article)<\/i> <b>34:<\/b> 15881-15885. <a href=\"http:\/\/doi.org\/10.1021\/bi00049a001\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1995BiochemPost.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Phelps, DK &amp; Post, CB. (1995) A novel basis of capsid stabilization by antiviral compounds. <i>J Mol Biol<\/i> <b>254:<\/b> 544-551.&nbsp;<a href=\"http:\/\/doi.org\/10.1006\/jmbi.1995.0637\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1995JMBPhelps.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB, Young, L &amp; Zheng, J. (1994) Conformational Equilibrium of Dihydronicotinamide in Ldh-Nadh. <i>Pure and Applied Chemistry<\/i> <b>66:<\/b> 83-88. <a href=\"http:\/\/library.iccs.edu\/cgi-bin\/koha\/opac-detail.pl?biblionumber=10705&amp;query_desc=callnum%3AQP-551-.P76-1993\" target=\"_blank\" rel=\"noopener noreferrer\">[link]<\/a><\/li>\n<li>Post, CB. (1994) Characterization of enzyme-complex formation by analysis of nuclear magnetic resonance line shapes. pp. 438-446 In <i>Methods Enzymol<\/i>, 1994\/01\/01 ed.&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1016\/S0076-6879(94)40058-X\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1994MethEnzPost.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Zheng, J &amp; Post, CB. (1993) Protein Indirect Relaxation Effects in Exchange-Transferred Noesy by a Rate-Matrix Analysis. <i>Journal of Magnetic Resonance Series B<\/i> <b>101:<\/b> 262-270.&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1006\/jmrb.1993.1042\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1993JMR-BZheng.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Young, L &amp; Post, CB. (1993) Free-Energy Calculations Involving Internal Coordinate Constraints to Determine Puckering of a 6-Membered Ring Molecule. <i>Journal of the American Chemical Society<\/i> <b>115:<\/b> 1964-1970. <a href=\"http:\/\/doi.org\/10.1021\/ja00058a050\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> [pdf]<\/li>\n<li>Ray, WJ, Jr., Post, CB &amp; Puvathingal, JM. (1993) Reaction of the isosteric methylenephosphonate analog of alpha-D-glucose 1-phosphate with phosphoglucomutase. Induced-fit specificity revisited. <i>Biochemistry<\/i> <b>32:<\/b> 38-47. <a href=\"http:\/\/doi.org\/10.1021\/bi00052a007\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1993BiochemRay.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Ray, WJ, Jr., Post, CB, Liu, Y &amp; Rhyu, GI. (1993) Structural changes at the metal ion binding site during the phosphoglucomutase reaction. <i>Biochemistry<\/i> <b>32:<\/b> 48-57. <a href=\"http:\/\/doi.org\/10.1021\/bi00052a008\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1993bBiochemRay.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB. (1992) Internal motional averaging and three-dimensional structure determination by nuclear magnetic resonance. <i>J Mol Biol<\/i> <b>224:<\/b> 1087-1101. <a href=\"http:\/\/doi.org\/0022-2836(92)90471-U\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1992JMBPost.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Meadows, RP, Kaluarachchi, K, Post, CB &amp; Gorenstein, DG. (1991) Just how accurate are structures determined from 2D NOESY spectra? The MORASS of an answer. <i>Bull. Magn. Reson.<\/i> <b>13:<\/b> 22-48.&nbsp;<a href=\"https:\/\/www.weizmann.ac.il\/ISMAR\/sites\/ISMAR\/files\/bulletin\/BMR_13_022-048_1991.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Ray, WJ, Jr. &amp; Post, CB. (1990) The oxyvanadium constellation in transition-state-analogue complexes of phosphoglucomutase and ribonuclease. Structural deductions from electron-transfer spectra. <i>Biochemistry<\/i> <b>29:<\/b> 2779-2789.&nbsp;<a href=\"http:\/\/doi.org\/10.1021\/bi00463a022\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1990BiochemRay.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Ray, WJ, Jr., Burgner, JW, 2nd &amp; Post, CB. (1990) Characterization of vanadate-based transition-state-analogue complexes of phosphoglucomutase by spectral and NMR techniques. <i>Biochemistry<\/i> <b>29:<\/b> 2770-2778.&nbsp;<a href=\"http:\/\/doi.org\/10.1021\/bi00463a021\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1990bBiochemRay.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB, Meadows, RP &amp; Gorenstein, DG. (1990) On the Evaluation of Interproton Distances for 3-Dimensional Structure Determination by Nmr Using a Relaxation Rate Matrix Analysis. <i>Journal of the American Chemical Society<\/i> <b>112:<\/b> 6796-6803. <a href=\"http:\/\/doi.org\/10.1021\/ja00175a009\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1990JACSPost.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB, Dobson, CM &amp; Karplus, M. (1990) Lysozyme Hydrolysis of Beta-Glycosides &#8211; a Consensus between Binding Interactions and Mechanism. pp. 377-388 In <i>Computer Modeling of Carbohydrate Molecules<\/i>. (eds. A.D. French, and J.W. Brady), ACS, Washington, DC. <a href=\"http:\/\/doi.org\/10.1021\/bk-1990-0430.ch023\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> [pdf]<\/li>\n<li>Gorenstein, DG, Meadows, RP, Metz, JT, Nikonowicz, E &amp; Post, CB. (1990) Phosphorus-31 and proton two-dimensional NMR and NOESY-distance restrained molecular dynamics methodologies for defining sequence-specific variations in duplex oligonucleotides: a comparison of NOESY two-spin approximation and the relaxation matrix analyses. <i>Adv. Biophys. Chem.<\/i> <b>1:<\/b> 47-124.&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/2523729\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> [pdf]<\/li>\n<li>Ray, WJ, Jr., Post, CB &amp; Puvathingal, JM. (1989) Comparison of rate constants for (PO3-) transfer by the Mg(II), Cd(II), and Li(I) forms of phosphoglucomutase. <i>Biochemistry<\/i> <b>28:<\/b> 559-569.&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/2523729\" target=\"_blank\" rel=\"noopener noreferrer\">[link]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1989BiochemRay.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB, Ray, WJ, Jr. &amp; Gorenstein, DG. (1989) Time-dependent 31P saturation transfer in the phosphoglucomutase reaction. Characterization of the spin system for the Cd(II) enzyme and evaluation of rate constants for the transfer process. <i>Biochemistry<\/i> <b>28:<\/b> 548-558.&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/2523728\" target=\"_blank\" rel=\"noopener noreferrer\">[link]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1989BiochemPost.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB, Dobson, CM &amp; Karplus, M. (1989) A molecular dynamics analysis of protein structural elements. <i>Proteins<\/i> <b>5:<\/b> 337-354.&nbsp;<a href=\"http:\/\/doi.org\/10.1002\/prot.340050409\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1989ProteinsPost.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB, Karplus, M &amp; Dobson, C. (1986) A lysozyme molecular dynamics simulation. <i>Ann. N. Y. Acad. Sci.<\/i> <b>482:<\/b> 267-268.<\/li>\n<li>Post, CB &amp; Karplus, M. (1986) Does Lysozyme Follow the Lysozyme Pathway &#8211; an Alternative Based on Dynamic, Structural, and Stereoelectronic Considerations. <i>Journal of the American Chemical Society<\/i> <b>108:<\/b> 1317-1319. <a href=\"http:\/\/doi.org\/10.1021\/ja00266a044\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1986JACSPost.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB, Brooks, BR, Karplus, M, Dobson, CM, Artymiuk, PJ, Cheetham, JC &amp; Phillips, DC. (1986) Molecular dynamics simulations of native and substrate-bound lysozyme. A study of the average structures and atomic fluctuations. <i>J Mol Biol<\/i> <b>190:<\/b> 455-479.&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1016\/0022-2836(86)90015-X\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> [pdf]<\/li>\n<li>Post, CB. (1984) A Monte-Carlo estimate of DNA loop formation. <i>Biopolymers<\/i> <b>23:<\/b> 601-605. <a href=\"http:\/\/doi.org\/10.1002\/bip.360230313\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1984BiopolymPost.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB. (1983) Excluded volume of an intermediate-molecular-weight DNA. A Monte Carlo analysis. <i>Biopolymers<\/i> <b>22:<\/b> 1087-1096. <a href=\"http:\/\/doi.org\/10.1002\/bip.360220406\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1983BiopolymPost.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB &amp; Zimm, BH. (1982) Theory of DNA condensation: collapse versus aggregation. <i>Biopolymers<\/i> <b>21:<\/b> 2123-2137. <a href=\"http:\/\/doi.org\/10.1002\/bip.360211104\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1982BiopolymersPost-cond.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB &amp; Zimm, BH. (1982) Light-scattering study of DNA condensation: competition between collapse and aggregation. <i>Biopolymers<\/i> <b>21:<\/b> 2139-2160.&nbsp;<a href=\"http:\/\/doi.org\/10.1002\/bip.360211105\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1982BiopolymersPost-ls.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB. (1981) <i>An analysis of DNA condensation<\/i>. Department of Chemistry University of California at San Diego, La Jolla, CA, 105 pp.<\/li>\n<li>Post, CB &amp; Zimm, BH. (1980) DNA condensation and how it relates to phase equilibrium in solution. <i>Biophys J<\/i> <b>32:<\/b> 448-4501327334.<a href=\"http:\/\/dx.doi.org\/10.1016\/S0006-3495(80)84977-0\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1980BJPost.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Post, CB &amp; Zimm, BH. (1979) Internal Condensation of a Single DNA Molecule. <i>Biopolymers<\/i> <b>18:<\/b> 1487-1501. <a href=\"http:\/\/doi.org\/10.1002\/bip.1979.360180612\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1979BiopolymPost.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<li>Wood, FE, Post, CB &amp; Cusanovich, MA. (1977) Reduction kinetics of bacterial cytochromes c2. <i>Arch Biochem Biophys<\/i> <b>184:<\/b> 586-595.&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1016\/0003-9861(77)90469-6\" target=\"_blank\" rel=\"noopener noreferrer\">[doi]<\/a> <a href=\"\/postlab\/wp-content\/uploads\/Publications\/1977AB&amp;BWood.pdf\" target=\"_blank\" rel=\"noopener noreferrer\">[pdf]<\/a><\/li>\n<\/ul>\n<\/div>\n","protected":false},"excerpt":{"rendered":"<p>Wu, H, Huang, H &amp; Post, CB. (2020) All-atom adaptively biased path optimization of Src kinase conformational inactivation: Switched electrostatic network in the concerted motion of \u03b1C helix and the activation loop.&nbsp;The Journal of Chemical Physics&nbsp;153: 175101. [doi]&#8230; <a class=\"read-more\" href=\"https:\/\/www.purdue.edu\/postlab\/publications\/\">Read More<\/a><\/p>\n","protected":false},"author":2,"featured_media":0,"parent":0,"menu_order":4,"comment_status":"closed","ping_status":"closed","template":"","meta":{"ngg_post_thumbnail":0,"footnotes":""},"class_list":["post-403","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/www.purdue.edu\/postlab\/wp-json\/wp\/v2\/pages\/403","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.purdue.edu\/postlab\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www.purdue.edu\/postlab\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www.purdue.edu\/postlab\/wp-json\/wp\/v2\/users\/2"}],"replies":[{"embeddable":true,"href":"https:\/\/www.purdue.edu\/postlab\/wp-json\/wp\/v2\/comments?post=403"}],"version-history":[{"count":34,"href":"https:\/\/www.purdue.edu\/postlab\/wp-json\/wp\/v2\/pages\/403\/revisions"}],"predecessor-version":[{"id":1190,"href":"https:\/\/www.purdue.edu\/postlab\/wp-json\/wp\/v2\/pages\/403\/revisions\/1190"}],"wp:attachment":[{"href":"https:\/\/www.purdue.edu\/postlab\/wp-json\/wp\/v2\/media?parent=403"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}