{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,19]],"date-time":"2025-10-19T06:03:00Z","timestamp":1760853780922},"reference-count":44,"publisher":"Public Library of Science (PLoS)","issue":"7","license":[{"start":{"date-parts":[[2014,7,31]],"date-time":"2014-07-31T00:00:00Z","timestamp":1406764800000},"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.1003721","type":"journal-article","created":{"date-parts":[[2014,7,31]],"date-time":"2014-07-31T15:22:26Z","timestamp":1406820146000},"page":"e1003721","update-policy":"http:\/\/dx.doi.org\/10.1371\/journal.pcbi.corrections_policy","source":"Crossref","is-referenced-by-count":21,"title":["Correlated Inter-Domain Motions in Adenylate Kinase"],"prefix":"10.1371","volume":"10","author":[{"given":"Santiago","family":"Esteban-Mart\u00edn","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robert Bryn","family":"Fenwick","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J\u00f6rgen","family":"\u00c5d\u00e9n","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Benjamin","family":"Cossins","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carlos W.","family":"Bertoncini","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Victor","family":"Guallar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Magnus","family":"Wolf-Watz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xavier","family":"Salvatella","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2014,7,31]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1038\/nature04105","article-title":"Intrinsic dynamics of an enzyme underlies catalysis","volume":"438","author":"EZ Eisenmesser","year":"2005","journal-title":"Nature"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1016\/j.sbi.2003.10.008","article-title":"The role of dynamics in allosteric regulation","volume":"13","author":"D Kern","year":"2003","journal-title":"Curr Opin Struct Biol"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"1042","DOI":"10.1016\/j.str.2009.06.008","article-title":"The Origin of Allosteric Functional Modulation: Multiple Pre-existing Pathways","volume":"17","author":"A del Sol","year":"2009","journal-title":"Structure"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"6155","DOI":"10.1021\/jp077018h","article-title":"Microsecond Molecular Dynamics Simulation Shows Effect of Slow Loop Dynamics on Backbone Amide Order Parameters of Proteins","volume":"112(19)","author":"P Maragakis","year":"2008","journal-title":"J Phys Chem B"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"2923","DOI":"10.1021\/ja0386804","article-title":"How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation?","volume":"126","author":"GM Clore","year":"2004","journal-title":"J Am Chem Soc"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"1471","DOI":"10.1126\/science.1157092","article-title":"Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution","volume":"320","author":"OF Lange","year":"2008","journal-title":"Science"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"10336","DOI":"10.1021\/ja200461n","article-title":"Weak Long-Range Correlated Motions in a Surface Patch of Ubiquitin Involved in Molecular Recognition","volume":"133","author":"RB Fenwick","year":"2011","journal-title":"J Am Chem Soc"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"10678","DOI":"10.1021\/bi049357w","article-title":"Amplitudes of protein backbone dynamics and correlated motions in a small alpha\/beta protein: correspondence of dipolar coupling and heteronuclear relaxation measurements","volume":"43","author":"GM Clore","year":"2004","journal-title":"Biochemistry"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"13885","DOI":"10.1073\/pnas.0505129102","article-title":"Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings","volume":"102","author":"G Bouvignies","year":"2005","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"3810","DOI":"10.1021\/ja8087295","article-title":"Toward an accurate determination of free energy landscapes in solution states of proteins","volume":"131","author":"A De Simone","year":"2009","journal-title":"J Am Chem Soc"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"1111","DOI":"10.1126\/science.278.5340.1111","article-title":"Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium","volume":"278","author":"N Tjandra","year":"1997","journal-title":"Science"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"3791","DOI":"10.1021\/ja0000908","article-title":"Prediction of Sterically Induced Alignment in a Dilute Liquid Crystalline Phase: Aid to Protein \u2026","volume":"122","author":"M Zweckstetter","year":"2000","journal-title":"J Am Chem Soc"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"9986","DOI":"10.1021\/ja026876i","article-title":"Physical interpretation of residual dipolar couplings in neutral aligned media","volume":"124","author":"A Almond","year":"2002","journal-title":"J Am Chem Soc"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"8961","DOI":"10.1021\/ja100447p","article-title":"Structural assembly of molecular complexes based on residual dipolar couplings","volume":"132","author":"K Berlin","year":"2010","journal-title":"J Am Chem Soc"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"886","DOI":"10.1126\/science.7754375","article-title":"Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling","volume":"268","author":"R Bruschweiler","year":"1995","journal-title":"Science"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1038\/nsb0697-443","article-title":"Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy","volume":"4","author":"N Tjandra","year":"1997","journal-title":"Nat Struct Biol"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"9522","DOI":"10.1021\/ja902336c","article-title":"Using the experimentally determined components of the overall rotational diffusion tensor to restrain molecular shape and size in NMR structure determination of globular proteins and protein-protein complexes","volume":"131","author":"Y Ryabov","year":"2009","journal-title":"J Am Chem Soc"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1017\/S0033583507004635","article-title":"X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution","volume":"40","author":"CD Putnam","year":"2007","journal-title":"Q Rev Biophys"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"6098","DOI":"10.1021\/ja010002z","article-title":"Model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins","volume":"123","author":"J Meiler","year":"2001","journal-title":"J Am Chem Soc"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1007\/s10858-007-9210-6","article-title":"Influence of the fluctuations of the alignment tensor on the analysis of the structure and dynamics of proteins using residual dipolar couplings","volume":"40","author":"X Salvatella","year":"2008","journal-title":"J Biomol NMR"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"052204","DOI":"10.1063\/1.2838167","article-title":"Conformational distributions of unfolded polypeptides from novel NMR techniques","volume":"128","author":"S Meier","year":"2008","journal-title":"J Chem Phys"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"4189","DOI":"10.1021\/ct200361b","article-title":"Determination of Conformational Equilibria in Proteins Using Residual Dipolar Couplings","volume":"7","author":"A De Simone","year":"2011","journal-title":"J Chem Theory Comput"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"17908","DOI":"10.1021\/ja9069024","article-title":"Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings","volume":"131","author":"G Nodet","year":"2009","journal-title":"J Am Chem Soc"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"1304","DOI":"10.1021\/ct0501811","article-title":"PELE: Protein Energy Landscape Exploration. A Novel Monte Carlo Based Technique","volume":"1","author":"KW Borrelli","year":"2005","journal-title":"J Chem Theory Comput"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"1911","DOI":"10.1021\/bi8018042","article-title":"Noncooperative folding of subdomains in adenylate kinase","volume":"48","author":"L Rundqvist","year":"2009","journal-title":"Biochemistry"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1038\/ncomms1106","article-title":"Overlap between folding and functional energy landscapes for adenylate kinase conformational change","volume":"1","author":"U Olsson","year":"2010","journal-title":"Nat Commun"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0969-2126(96)00018-4","article-title":"Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding","volume":"4","author":"CW M\u00fcller","year":"1996","journal-title":"Structure"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"838","DOI":"10.1038\/nature06410","article-title":"Intrinsic motions along an enzymatic reaction trajectory","volume":"450","author":"KA Henzler-Wildman","year":"2007","journal-title":"Nature"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"18055","DOI":"10.1073\/pnas.0708600104","article-title":"Illuminating the mechanistic roles of enzyme conformational dynamics","volume":"104","author":"JA Hanson","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"14003","DOI":"10.1021\/ja075055g","article-title":"NMR identification of transient complexes critical to adenylate kinase catalysis","volume":"129","author":"J Ad\u00e9n","year":"2007","journal-title":"J Am Chem Soc"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/0022-2836(92)90582-5","article-title":"Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state","volume":"224","author":"CW M\u00fcller","year":"1992","journal-title":"J Mol Biol"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"16984","DOI":"10.1073\/pnas.0906510106","article-title":"Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins","volume":"106","author":"TP Schrank","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"2042","DOI":"10.1074\/jbc.M707632200","article-title":"Conformational transitions in adenylate kinase. Allosteric communication reduces misligation","volume":"283","author":"PC Whitford","year":"2008","journal-title":"J Biol Chem"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"1661","DOI":"10.1016\/j.jmb.2006.11.085","article-title":"Conformational transitions of adenylate kinase: switching by cracking","volume":"366","author":"PC Whitford","year":"2007","journal-title":"J Mol Biol"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1016\/j.str.2008.04.013","article-title":"The atomistic mechanism of conformational transition in adenylate kinase: a TEE-REX molecular dynamics study","volume":"16","author":"MB Kubitzki","year":"2008","journal-title":"Structure"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"18496","DOI":"10.1073\/pnas.0706443104","article-title":"Large-scale allosteric conformational transitions of adenylate kinase appear to involve a population-shift mechanism","volume":"104","author":"K Arora","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/S0014-5793(96)01195-7","article-title":"Towards a mechanism of AMP-substrate inhibition in adenylate kinase from Escherichia coli","volume":"397","author":"MA Sinev","year":"1996","journal-title":"FEBS Lett"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.jmb.2009.09.009","article-title":"Zipping and unzipping of adenylate kinase: atomistic insights into the ensemble of open\/closed transitions","volume":"394","author":"O Beckstein","year":"2009","journal-title":"J Mol Biol"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"9013","DOI":"10.1021\/bi9905213","article-title":"Domain orientation and dynamics in multidomain proteins from residual dipolar couplings","volume":"38","author":"MW Fischer","year":"1999","journal-title":"Biochemistry"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1023\/A:1024733922459","article-title":"NMR studies of structure and function of biological macromolecules (Nobel Lecture)","volume":"27","author":"K W\u00fcthrich","year":"2003","journal-title":"J Biomol NMR"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"15927","DOI":"10.1021\/ja804274s","article-title":"16-fold degeneracy of peptide plane orientations from residual dipolar couplings: analytical treatment and implications for protein structure determination","volume":"130","author":"J-C Hus","year":"2008","journal-title":"J Am Chem Soc"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1038\/nchem.1124","article-title":"Protein dynamics: whispering within","volume":"3","author":"R Br\u00fcschweiler","year":"2011","journal-title":"Nat Chem"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"6836","DOI":"10.1021\/ja9812610","article-title":"Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid \u2026","volume":"120","author":"G Cornilescu","year":"1998","journal-title":"J Am Chem Soc"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"1545","DOI":"10.1002\/jcc.21287","article-title":"CHARMM: the biomolecular simulation program","volume":"30","author":"BR Brooks","year":"2009","journal-title":"J Comput Chem"}],"container-title":["PLoS Computational Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pcbi.1003721","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2018,10,23]],"date-time":"2018-10-23T02:24:41Z","timestamp":1540261481000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pcbi.1003721"}},"subtitle":[],"editor":[{"given":"Helmut","family":"Grubm\u00fcller","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2014,7,31]]},"references-count":44,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2014,7,31]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pcbi.1003721","relation":{},"ISSN":["1553-7358"],"issn-type":[{"value":"1553-7358","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,7,31]]}}}