{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,14]],"date-time":"2026-04-14T02:08:13Z","timestamp":1776132493294,"version":"3.50.1"},"reference-count":79,"publisher":"Public Library of Science (PLoS)","issue":"9","license":[{"start":{"date-parts":[[2011,9,29]],"date-time":"2011-09-29T00:00:00Z","timestamp":1317254400000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.ploscompbiol.org"],"crossmark-restriction":false},"short-container-title":["PLoS Comput Biol"],"DOI":"10.1371\/journal.pcbi.1002201","type":"journal-article","created":{"date-parts":[[2011,9,29]],"date-time":"2011-09-29T16:40:16Z","timestamp":1317314416000},"page":"e1002201","update-policy":"https:\/\/doi.org\/10.1371\/journal.pcbi.corrections_policy","source":"Crossref","is-referenced-by-count":52,"title":["Changes in Dynamics upon Oligomerization Regulate Substrate Binding and Allostery in Amino Acid Kinase Family Members"],"prefix":"10.1371","volume":"7","author":[{"given":"Enrique","family":"Marcos","sequence":"first","affiliation":[]},{"given":"Ramon","family":"Crehuet","sequence":"additional","affiliation":[]},{"given":"Ivet","family":"Bahar","sequence":"additional","affiliation":[]}],"member":"340","published-online":{"date-parts":[[2011,9,29]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"964","DOI":"10.1038\/nature06522","article-title":"Dynamic personalities of proteins.","volume":"450","author":"K Henzler-Wildman","year":"2007","journal-title":"Nature"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1006\/jmbi.1999.3419","article-title":"Relationships between protein structure and dynamics from a database of NMR-derived backbone order parameters.","volume":"295","author":"JL Goodman","year":"2000","journal-title":"J Mol Biol"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"12654","DOI":"10.1021\/ja027847a","article-title":"Contact model for the prediction of NMR N-H order parameters in globular proteins.","volume":"124","author":"FL Zhang","year":"2002","journal-title":"J Am Chem Soc"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"18908","DOI":"10.1073\/pnas.0507603102","article-title":"Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state.","volume":"102","author":"D Tobi","year":"2005","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"14349","DOI":"10.1073\/pnas.0904214106","article-title":"The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding.","volume":"106","author":"A Bakan","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1146\/annurev.biophys.093008.131258","article-title":"Global Dynamics of Proteins: Bridging Between Structure and Function.","volume":"39","author":"I Bahar","year":"2010","journal-title":"Annu Rev Biophys"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1146\/annurev.biophys.35.040405.102010","article-title":"Symmetry, form, and shape: Guiding principles for robustness in macromolecular machines.","volume":"35","author":"F Tama","year":"2006","journal-title":"Annu Rev Biophys Biomol Struct"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1016\/j.bpj.2009.05.033","article-title":"Enzymatic Activity versus Structural Dynamics: The Case of Acetylcholinesterase Tetramer.","volume":"97","author":"AA Gorfe","year":"2009","journal-title":"Biophys J"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"1274","DOI":"10.1073\/pnas.032522499","article-title":"Flexibility and packing in proteins.","volume":"99","author":"B Halle","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1093\/protein\/14.1.1","article-title":"Conformational change of proteins arising from normal mode calculations.","volume":"14","author":"F Tama","year":"2001","journal-title":"Protein Eng"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1038\/nsmb821","article-title":"Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair.","volume":"11","author":"M Wolf-Watz","year":"2004","journal-title":"Nat Struct Mol Biol"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"1520","DOI":"10.1126\/science.1066176","article-title":"Enzyme dynamics during catalysis.","volume":"295","author":"EZ Eisenmesser","year":"2002","journal-title":"Science"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"1422","DOI":"10.1002\/chem.200801223","article-title":"Protein Flexibility and Metal Coordination Changes in DHAP-Dependent Aldolases.","volume":"15","author":"A Jimenez","year":"2009","journal-title":"Chemistry-a European Journal"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1021\/bi7012799","article-title":"Antenna domain mobility and enzymatic reaction of L-rhamnulose-1-phosphate aldolase.","volume":"47","author":"D Grueninger","year":"2008","journal-title":"Biochemistry"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1038\/nature06407","article-title":"A hierarchy of timescales in protein dynamics is linked to enzyme catalysis.","volume":"450","author":"KA Henzler-Wildman","year":"2007","journal-title":"Nature"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1017\/S0033583500003826","article-title":"Mechanisms of cooperativty and allosteric regulation in proteins.","volume":"22","author":"MF Perutz","year":"1989","journal-title":"Q Rev Biophys"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"4472","DOI":"10.1073\/pnas.88.10.4472","article-title":"Application of linear free-energy relations to protein conformational changes: the quaternary structural change of hemoglobin.","volume":"88","author":"WA Eaton","year":"1991","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.jmb.2003.08.027","article-title":"Allosteric changes in protein structure computed by a simple mechanical model: Hemoglobin T &lt;-&gt; R2 transition.","volume":"333","author":"CY Xu","year":"2003","journal-title":"J Mol Biol"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"1424","DOI":"10.1126\/science.1108595","article-title":"Allosteric mechanisms of signal transduction.","volume":"308","author":"JP Changeux","year":"2005","journal-title":"Science"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1006\/jmbi.1996.0257","article-title":"Motions in hemoglobin studied by normal mode analysis and energy minimization: Evidence for the existence of tertiary T-like, quaternary R-like intermediate structures.","volume":"258","author":"L Mouawad","year":"1996","journal-title":"J Mol Biol"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1021\/bi00865a047","article-title":"Comparison of experimental binding data and theoretical models in proteins containing subunits.","volume":"5","author":"DE Koshland","year":"1966","journal-title":"Biochemistry"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/S0022-2836(65)80285-6","article-title":"On nature of allosteric transitions - A plausible model.","volume":"12","author":"J Monod","year":"1965","journal-title":"J Mol Biol"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1111\/j.1747-0285.2011.01101.x","article-title":"Applying molecular dynamics simulations to identify rarely sampled ligand-bound conformational states of undecaprenyl pyrophosphate synthase, an antibacterial target.","volume":"77","author":"W Sinko","year":"2011","journal-title":"Chem Biol Drug Des"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1073\/pnas.93.1.13","article-title":"Principles of protein-protein interactions.","volume":"93","author":"S Jones","year":"1996","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1021\/cr960387h","article-title":"Protein-protein interactions: Interface structure, binding thermodynamics, and mutational analysis.","volume":"97","author":"WE Stites","year":"1997","journal-title":"Chem Rev"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"934","DOI":"10.1110\/ps.8.4.934","article-title":"Carbamate kinase: New structural machinery for making carbamoyl phosphate, the common precursor of pyrimidines and arginine.","volume":"8","author":"A Marina","year":"1999","journal-title":"Protein Sci"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1006\/jmbi.2000.3779","article-title":"The 1.5 angstrom resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases.","volume":"299","author":"S Ramon-Maiques","year":"2000","journal-title":"J Mol Biol"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/S0969-2126(02)00721-9","article-title":"Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis.","volume":"10","author":"S Ramon-Maiques","year":"2002","journal-title":"Structure"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1016\/j.jmb.2005.07.045","article-title":"The crystal structure of Pyrococcus furiosus UMP kinase provides insight into catalysis and regulation in microbial pyrimidine nucleotide biosynthesis.","volume":"352","author":"C Marco-Marin","year":"2005","journal-title":"J Mol Biol"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1016\/j.jmb.2005.11.079","article-title":"Structural bases of feed-back control of arginine biosynthesis, revealed by the structures of two hexameric N-acetylglutamate kinases, from Thermotoga maritima and Pseudomonas aeruginosa.","volume":"356","author":"S Ramon-Maiques","year":"2006","journal-title":"J Mol Biol"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"1431","DOI":"10.1016\/j.jmb.2007.01.073","article-title":"A novel two-domain architecture within the amino acid kinase enzyme family revealed by the crystal structure of Escherichia coli glutamate 5-kinase.","volume":"367","author":"C Marco-Marin","year":"2007","journal-title":"J Mol Biol"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1016\/j.jmb.2010.04.025","article-title":"Two Crystal Structures of Escherichia coli N-Acetyl-L-Glutamate Kinase Demonstrate the Cycling between Open and Closed Conformations.","volume":"399","author":"F Gil-Ortiz","year":"2010","journal-title":"J Mol Biol"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/S0022-2836(03)00716-2","article-title":"The course of phosphorus in the reaction of N-acetyl-L-glutamate kinase, determined from the structures of crystalline complexes, including a complex with an AlF4- transition state mimic.","volume":"331","author":"F Gil-Ortiz","year":"2003","journal-title":"J Mol Biol"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"e1000738","DOI":"10.1371\/journal.pcbi.1000738","article-title":"On the Conservation of the Slow Conformational Dynamics within the Amino Acid Kinase Family: NAGK the Paradigm.","volume":"6","author":"E Marcos","year":"2010","journal-title":"PLoS Comput Biol"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"17644","DOI":"10.1073\/pnas.0705987104","article-title":"The crystal structure of the complex of P-II and acetylglutamate kinase reveals how P-II controls the storage of nitrogen as arginine.","volume":"104","author":"JL Llacer","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"3018","DOI":"10.1128\/JB.01831-07","article-title":"Basis of arginine sensitivity of microbial N-acetyl-L-glutamate kinases: Mutagenesis and protein engineering study with the Pseudomonas aeruginosa and Escherichia coli enzymes.","volume":"190","author":"ML Fernandez-Murga","year":"2008","journal-title":"J Bacteriol"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"1261","DOI":"10.1016\/j.jmb.2010.02.038","article-title":"Substrate Binding and Catalysis in Carbamate Kinase Ascertained by Crystallographic and Site-Directed Mutagenesis Studies: Movements and Significance of a Unique Globular Subdomain of This Key Enzyme for Fermentative ATP Production in Bacteria.","volume":"397","author":"S Ramon-Maiques","year":"2010","journal-title":"J Mol Biol"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"5013","DOI":"10.1016\/j.bmc.2005.05.037","article-title":"Protein oligomerization: How and why.","volume":"13","author":"MH Ali","year":"2005","journal-title":"Bioorg Med Chem"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1126\/science.1150421","article-title":"Designed protein-protein association.","volume":"319","author":"D Grueninger","year":"2008","journal-title":"Science"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1016\/S0006-3495(01)76033-X","article-title":"Anisotropy of fluctuation dynamics of proteins with an elastic network model.","volume":"80","author":"AR Atilgan","year":"2001","journal-title":"Biophys J"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"2619","DOI":"10.1093\/bioinformatics\/btl448","article-title":"Anisotropic network model: systematic evaluation and a new web interface.","volume":"22","author":"E Eyal","year":"2006","journal-title":"Bioinformatics"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1002\/prot.10168","article-title":"Normal mode analysis of macromolecular motions in a database framework: Developing mode concentration as a useful classifying statistic.","volume":"48","author":"WG Krebs","year":"2002","journal-title":"Proteins"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/j.str.2007.12.011","article-title":"Close correspondence between the motions from principal component analysis of multiple HIV-1 protease structures and elastic network modes.","volume":"16","author":"L Yang","year":"2008","journal-title":"Structure"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1093\/bioinformatics\/btp023","article-title":"Principal component analysis of native ensembles of biomolecular structures (PCA_NEST): insights into functional dynamics.","volume":"25","author":"LW Yang","year":"2009","journal-title":"Bioinformatics"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"1070","DOI":"10.1006\/jmbi.1996.0224","article-title":"Analysis of the low frequency normal modes of the T-state of aspartate transcarbamylase.","volume":"257","author":"A Thomas","year":"1996","journal-title":"J Mol Biol"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"128","DOI":"10.2174\/138920309787847608","article-title":"Allosteric Transitions in Biological Nanomachines are Described by Robust Normal Modes of Elastic Networks.","volume":"10","author":"WJ Zheng","year":"2009","journal-title":"Current Protein & Peptide Science"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1016\/j.str.2007.03.013","article-title":"Thorough validation of protein normal mode analysis: A comparative study with essential dynamics.","volume":"15","author":"M Rueda","year":"2007","journal-title":"Structure"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1002\/prot.22518","article-title":"A comparative analysis of the equilibrium dynamics of a designed protein inferred from NMR, X-ray, and computations.","volume":"77","author":"L Liu","year":"2009","journal-title":"Proteins"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1002\/prot.22855","article-title":"Validating and improving elastic network models with molecular dynamics simulations.","volume":"79","author":"TD Romo","year":"2011","journal-title":"Proteins"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1002\/prot.21787","article-title":"Influence of oligomerization on the dynamics of G-protein coupled receptors as assessed by normal mode analysis.","volume":"71","author":"MY Niv","year":"2008","journal-title":"Proteins"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"3399","DOI":"10.1529\/biophysj.105.064840","article-title":"Comparison of tRNA motions in the free and ribosomal bound structures.","volume":"89","author":"YM Wang","year":"2005","journal-title":"Biophys J"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1529\/biophysj.106.077800","article-title":"Cooperative fluctuations point to the dimerization interface of p53 core domain.","volume":"91","author":"N Kantarci","year":"2006","journal-title":"Biophys J"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1002\/(SICI)1097-0134(19980815)32:3<324::AID-PROT8>3.0.CO;2-H","article-title":"Dynamic structure of subtilisin-eglin c complex studied by normal mode analysis.","volume":"32","author":"H Ishida","year":"1998","journal-title":"Proteins"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"e1000360","DOI":"10.1371\/journal.pcbi.1000360","article-title":"Allosteric Transitions of Supramolecular Systems Explored by Network Models: Application to Chaperonin GroEL.","volume":"5","author":"Z Yang","year":"2009","journal-title":"PLoS Comput Biol"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","article-title":"Inference of macromolecular assemblies from crystalline state.","volume":"372","author":"E Krissinel","year":"2007","journal-title":"J Mol Biol"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"2780","DOI":"10.1093\/bioinformatics\/btn507","article-title":"Searching protein structure databases with DaliLite v.3.","volume":"24","author":"L Holm","year":"2008","journal-title":"Bioinformatics"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"2194","DOI":"10.1002\/pro.5560031205","article-title":"Cavities and packing at protein interfaces.","volume":"3","author":"SJ Hubbard","year":"1994","journal-title":"Protein Sci"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"25533","DOI":"10.1074\/jbc.M501849200","article-title":"Structure of Escherichia coli UMP kinase differs from that of other nucleoside monophosphate kinases and sheds new light on enzyme regulation.","volume":"280","author":"P Briozzo","year":"2005","journal-title":"J Biol Chem"},{"key":"ref59","doi-asserted-by":"crossref","first-page":"36011","DOI":"10.1074\/jbc.M802614200","article-title":"Structural and Functional Characterization of Escherichia coli UMP Kinase in Complex with Its Allosteric Regulator GTP.","volume":"283","author":"P Meyer","year":"2008","journal-title":"J Biol Chem"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"3458","DOI":"10.1093\/nar\/gkq1250","article-title":"Structural and functional characterization of the Mycobacterium tuberculosis uridine monophosphate kinase: insights into the allosteric regulation.","volume":"39","author":"G Labesse","year":"2011","journal-title":"Nucleic Acids Res"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/S0301-0104(00)00222-6","article-title":"Harmonicity in slow protein dynamics.","volume":"261","author":"K Hinsen","year":"2000","journal-title":"Chem Phys"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"2457","DOI":"10.1016\/S0006-3495(02)75257-0","article-title":"A coarse-grained normal mode approach for macromolecules: An efficient implementation and application to Ca2+-ATPase.","volume":"83","author":"GH Li","year":"2002","journal-title":"Biophys J"},{"key":"ref63","doi-asserted-by":"crossref","first-page":"W610","DOI":"10.1093\/nar\/gkh368","article-title":"ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement.","volume":"32","author":"K Suhre","year":"2004","journal-title":"Nucleic Acids Res"},{"key":"ref64","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/S1359-0278(97)00024-2","article-title":"Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential.","volume":"2","author":"I Bahar","year":"1997","journal-title":"Fold Des"},{"key":"ref65","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1016\/j.sbi.2005.08.007","article-title":"Coarse-grained normal mode analysis in structural biology.","volume":"15","author":"I Bahar","year":"2005","journal-title":"Curr Opin Struct Biol"},{"key":"ref66","doi-asserted-by":"crossref","first-page":"078104","DOI":"10.1103\/PhysRevLett.96.078104","article-title":"Functional modes of proteins are among the most robust.","volume":"96","author":"S Nicolay","year":"2006","journal-title":"Phys Rev Lett"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1016\/S0006-3495(02)75203-X","article-title":"Dynamics of proteins in crystals: Comparison of experiment with simple models.","volume":"83","author":"S Kundu","year":"2002","journal-title":"Biophys J"},{"key":"ref68","doi-asserted-by":"crossref","first-page":"7693","DOI":"10.1021\/bi060652l","article-title":"Dynamic coupling and allosteric behavior in a nonallosteric protein.","volume":"45","author":"MW Clarkson","year":"2006","journal-title":"Biochemistry"},{"key":"ref69","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1038\/nchembio.98","article-title":"Allosteric regulation and catalysis emerge via a common route.","volume":"4","author":"NM Goodey","year":"2008","journal-title":"Nat Chem Biol"},{"key":"ref70","doi-asserted-by":"crossref","first-page":"2794","DOI":"10.1073\/pnas.052005999","article-title":"Network of coupled promoting motions in enzyme catalysis.","volume":"99","author":"PK Agarwal","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref71","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1038\/nsb881","article-title":"Evolutionarily conserved networks of residues mediate allosteric communication in proteins.","volume":"10","author":"GM Suel","year":"2003","journal-title":"Nat Struct Biol"},{"key":"ref72","doi-asserted-by":"crossref","first-page":"2776","DOI":"10.1016\/j.febslet.2007.05.021","article-title":"Network analysis of protein dynamics.","volume":"581","author":"C Bode","year":"2007","journal-title":"FEBS Lett"},{"key":"ref73","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1038\/msb4100075","article-title":"Markov propagation of allosteric effects in biomolecular systems: application to GroEL-GroES.","volume":"2","author":"C Chennubhotla","year":"2006","journal-title":"Mol Syst Biol"},{"key":"ref74","first-page":"1716","article-title":"Signal propagation in proteins and relation to equilibrium fluctuations.","volume":"3","author":"C Chennubhotla","year":"2007","journal-title":"PLoS Comput Biol"},{"key":"ref75","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1529\/biophysj.105.063305","article-title":"Probing the local dynamics of nucleotide-binding pocket coupled to the global dynamics: Myosin versus kinesin.","volume":"89","author":"WJ Zheng","year":"2005","journal-title":"Biophys J"},{"key":"ref76","doi-asserted-by":"crossref","first-page":"198103","DOI":"10.1103\/PhysRevLett.95.198103","article-title":"Allostery in a coarse-grained model of protein dynamics.","volume":"95","author":"D Ming","year":"2005","journal-title":"Phys Rev Lett"},{"key":"ref77","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/j.jmb.2006.01.097","article-title":"Interactions in native binding sites cause a large change in protein dynamics.","volume":"358","author":"DM Ming","year":"2006","journal-title":"J Mol Biol"},{"key":"ref78","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1002\/1096-987X(200103)22:4<387::AID-JCC1010>3.0.CO;2-R","article-title":"On the quadratic reaction path evaluated in a reduced potential energy surface model and the problem to locate transition states.","volume":"22","author":"JM Anglada","year":"2001","journal-title":"J Comput Chem"},{"key":"ref79","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: Visual molecular dynamics.","volume":"14","author":"W Humphrey","year":"1996","journal-title":"J Mol Graph"}],"container-title":["PLoS Computational Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pcbi.1002201","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2018,10,23]],"date-time":"2018-10-23T16:53:16Z","timestamp":1540313596000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pcbi.1002201"}},"subtitle":[],"editor":[{"given":"Michael","family":"Gilson","sequence":"first","affiliation":[]}],"short-title":[],"issued":{"date-parts":[[2011,9,29]]},"references-count":79,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2011,9,29]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pcbi.1002201","relation":{},"ISSN":["1553-7358"],"issn-type":[{"value":"1553-7358","type":"electronic"}],"subject":[],"published":{"date-parts":[[2011,9,29]]}}}