{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T09:16:10Z","timestamp":1772356570826,"version":"3.50.1"},"reference-count":78,"publisher":"Public Library of Science (PLoS)","issue":"5","license":[{"start":{"date-parts":[[2016,5,10]],"date-time":"2016-05-10T00:00:00Z","timestamp":1462838400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/publicdomain\/zero\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000062","name":"National Institute of Diabetes and Digestive and Kidney Diseases","doi-asserted-by":"publisher","award":["Intramural Award"],"award-info":[{"award-number":["Intramural Award"]}],"id":[{"id":"10.13039\/100000062","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.ploscompbiol.org"],"crossmark-restriction":false},"short-container-title":["PLoS Comput Biol"],"DOI":"10.1371\/journal.pcbi.1004933","type":"journal-article","created":{"date-parts":[[2016,5,10]],"date-time":"2016-05-10T17:34:41Z","timestamp":1462901681000},"page":"e1004933","update-policy":"https:\/\/doi.org\/10.1371\/journal.pcbi.corrections_policy","source":"Crossref","is-referenced-by-count":41,"title":["Structural Determinants of Misfolding in Multidomain Proteins"],"prefix":"10.1371","volume":"12","author":[{"given":"Pengfei","family":"Tian","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robert B.","family":"Best","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2016,5,10]]},"reference":[{"issue":"6968","key":"ref1","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1038\/nature02261","article-title":"Protein folding and misfolding","volume":"426","author":"CM Dobson","year":"2003","journal-title":"Nature"},{"key":"ref2","first-page":"137","article-title":"Protein Dimerization and Oligomerization in Biology","author":"F Rousseau","year":"2012"},{"issue":"2","key":"ref3","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1006\/jmbi.2001.4776","article-title":"Domain combinations in archaeal, eubacterial and eukaryotic proteomes","volume":"310","author":"G Apic","year":"2001","journal-title":"J Mol Biol"},{"issue":"1","key":"ref4","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/j.jmb.2005.02.007","article-title":"Multi-domain proteins in the three kingdoms of life: orphan domains and other unassigned regions","volume":"348","author":"D Ekman","year":"2005","journal-title":"J Mol Biol"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"1954","DOI":"10.1016\/j.str.2013.08.028","article-title":"Complex energy landscape of a giant repeat protein","volume":"21","author":"M Tsytlonok","year":"2013","journal-title":"Structure"},{"issue":"4","key":"ref6","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1038\/nrm2144","article-title":"The folding and evolution of multidomain proteins","volume":"8","author":"JH Han","year":"2007","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"7353","key":"ref7","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1038\/nature10099","article-title":"Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins","volume":"474","author":"MB Borgia","year":"2011","journal-title":"Nature"},{"issue":"11","key":"ref8","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1038\/14907","article-title":"Single protein misfolding events captured by atomic force microscopy","volume":"6","author":"AF Oberhauser","year":"1999","journal-title":"Nat Struct Biol"},{"issue":"4","key":"ref9","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1016\/j.jmb.2011.07.049","article-title":"Kinetic partitioning mechanism governs the folding of the third FnIII domain of tenascin-C: evidence at the single-molecule level","volume":"412","author":"Q Peng","year":"2011","journal-title":"J Mol Biol"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"4226","DOI":"10.1074\/jbc.M115.673871","article-title":"Single molecule force spectroscopy predicts a misfolded, domain-swapped conformation in human <italic>\u03b3<\/italic>D-crystallin","volume":"291","author":"S Garcia-Manyes","year":"2015","journal-title":"J Biol Chem"},{"issue":"5","key":"ref11","doi-asserted-by":"crossref","first-page":"1680","DOI":"10.1073\/pnas.1222130110","article-title":"Frustration in the energy landscapes of multidomain protein misfolding","volume":"110","author":"W Zheng","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref12","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms9861","article-title":"Transient misfolding dominates multidomain protein folding","volume":"6","author":"A Borgia","year":"2015","journal-title":"Nat Commun"},{"issue":"9","key":"ref13","doi-asserted-by":"crossref","first-page":"1881","DOI":"10.1110\/ps.05801","article-title":"Circularly permuted proteins in the protein structure database","volume":"10","author":"J Jung","year":"2001","journal-title":"Protein Sci"},{"issue":"2","key":"ref14","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1038\/nmat1825","article-title":"Polyprotein of GB1 is an ideal artificial elastomeric protein","volume":"6","author":"Y Cao","year":"2007","journal-title":"Nat Mater"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"1674","DOI":"10.1126\/science.1092497","article-title":"Force clamp spectroscopy monitors the folding trajectory of a single protein","volume":"303","author":"JM Fernandez","year":"2004","journal-title":"Science"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"411b","DOI":"10.1126\/science.1100962","article-title":"Force clamp spectroscopy monitors the folding trajectory of a single protein","volume":"306","author":"TR Sosnick","year":"2004","journal-title":"Science"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"411c","DOI":"10.1126\/science.1102236","article-title":"Force clamp spectroscopy monitors the folding trajectory of a single protein","volume":"306","author":"JM Fernandez","year":"2004","journal-title":"Science"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"498b","DOI":"10.1126\/science.1106969","article-title":"Force-clamp spectroscopy monitors the folding trajectory of a single protein","volume":"308","author":"RB Best","year":"2005","journal-title":"Science"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"3706","DOI":"10.1021\/ja0762691","article-title":"Protein folding kinetics under force from molecular simulation","volume":"130","author":"RB Best","year":"2008","journal-title":"J Am Chem Soc"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"498c","DOI":"10.1126\/science.1107675","article-title":"Force clamp spectroscopy monitors the folding trajectory of a single protein","volume":"308","author":"J Brujic","year":"2005","journal-title":"Science"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"820","DOI":"10.1002\/anie.200804723","article-title":"Surprising simplicity in the single-molecule folding mechanics of proteins","volume":"48","author":"M Schlierf","year":"2009","journal-title":"Angew Chem"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"10534","DOI":"10.1073\/pnas.0901213106","article-title":"Direct observation of an ensemble of stable collapsed states in the mechanical folding of ubiquitin","volume":"106","author":"S Garcia-Manyes","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"6963","DOI":"10.1073\/pnas.1018177108","article-title":"Minimum energy compact structures in force-quench polyubiquitin folding are domain swapped","volume":"108","author":"F Xia","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"7069","key":"ref24","doi-asserted-by":"crossref","first-page":"878","DOI":"10.1038\/nature04195","article-title":"The importance of sequence diversity in the aggregation and evolution of proteins","volume":"438","author":"CF Wright","year":"2005","journal-title":"Nature"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"4938","DOI":"10.2741\/3053","article-title":"The SH3 domain\u2013a family of versatile peptide-and protein-recognition module","volume":"13","author":"T Kaneko","year":"2008","journal-title":"Front Biosci"},{"issue":"4","key":"ref26","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1016\/S0022-2836(05)80146-9","article-title":"The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics","volume":"247","author":"AR Viguera","year":"1995","journal-title":"J Mol Biol"},{"issue":"1","key":"ref27","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/0959-437X(94)90087-6","article-title":"SH2\/SH3 signaling proteins","volume":"4","author":"J Schlessinger","year":"1994","journal-title":"Curr Opin Gen Dev"},{"issue":"44","key":"ref28","doi-asserted-by":"crossref","first-page":"13376","DOI":"10.1021\/bi0012336","article-title":"Dimer formation through domain swapping in the crystal structure of the Grb2-SH2-Ac-pYVNV complex","volume":"39","author":"N Schiering","year":"2000","journal-title":"Biochemistry"},{"issue":"1","key":"ref29","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.abb.2007.03.010","article-title":"Structural and energetic aspects of Grb2-SH2 domain-swapping","volume":"462","author":"AP Benfield","year":"2007","journal-title":"Arch Biochem Biophys"},{"issue":"45","key":"ref30","doi-asserted-by":"crossref","first-page":"17668","DOI":"10.1073\/pnas.0707977104","article-title":"High-resolution design of a protein loop","volume":"104","author":"X Hu","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"2","key":"ref31","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1002\/pro.5560060225","article-title":"Evidence for PDZ domains in bacteria, yeast, and plants","volume":"6","author":"CP Ponting","year":"1997","journal-title":"Protein Sci"},{"issue":"18","key":"ref32","doi-asserted-by":"crossref","first-page":"3219","DOI":"10.1242\/jcs.114.18.3219","article-title":"Mechanism and role of PDZ domains in signaling complex assembly","volume":"114","author":"BZ Harris","year":"2001","journal-title":"J Cell Sci"},{"issue":"9","key":"ref33","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1038\/78973","article-title":"Crystal structures of the photosystem II D1 C-terminal processing protease","volume":"7","author":"DI Liao","year":"2000","journal-title":"Nat Struct Mol Biol"},{"issue":"14","key":"ref34","doi-asserted-by":"crossref","first-page":"8954","DOI":"10.1074\/jbc.M707424200","article-title":"Folding and misfolding in a naturally occurring circularly permuted PDZ domain","volume":"283","author":"Y Ivarsson","year":"2008","journal-title":"J Biol Chem"},{"issue":"3","key":"ref35","doi-asserted-by":"crossref","first-page":"e1002445","DOI":"10.1371\/journal.pcbi.1002445","article-title":"Circular permutation in proteins","volume":"8","author":"S Bliven","year":"2012","journal-title":"PLoS Comput Biol"},{"issue":"49","key":"ref36","doi-asserted-by":"crossref","first-page":"35988","DOI":"10.1074\/jbc.M703826200","article-title":"Domain-swapped dimerization of the second PDZ domain of ZO2 may provide a structural basis for the polymerization of claudins","volume":"282","author":"J Wu","year":"2007","journal-title":"J Biol Chem"},{"key":"ref37","first-page":"20","article-title":"PDZ domains and their binding partners: structure, specificity, and modification","volume":"7","author":"HJ Lee","year":"2010","journal-title":"Interactions"},{"issue":"3","key":"ref38","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1161\/01.RES.0000117769.88862.F8","article-title":"The giant protein titin a major player in myocardial mechanics, signaling, and disease","volume":"94","author":"HL Granzier","year":"2004","journal-title":"Circulation Res"},{"issue":"9","key":"ref39","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1038\/nrm1198","article-title":"Titin: properties and family relationships","volume":"4","author":"L Tskhovrebova","year":"2003","journal-title":"Nat Rev Mol Cell Biol"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1038\/35056563","article-title":"Themes and variations on ubiquitylation","volume":"2","author":"AM Weissman","year":"2001","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"10","key":"ref41","doi-asserted-by":"crossref","first-page":"2351","DOI":"10.1110\/ps.0205402","article-title":"The origins of asymmetry in the folding transition states of protein L and protein G","volume":"11","author":"J Karanicolas","year":"2002","journal-title":"Protein Sci"},{"issue":"3","key":"ref42","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1021\/ct700301q","article-title":"GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation","volume":"4","author":"B Hess","year":"2008","journal-title":"J Chem Theor Comput"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1038\/359851a0","article-title":"Crystal structure of a Src-homology 3 (SH3) domain","volume":"351","author":"A Musacchio","year":"1992","journal-title":"Nature"},{"issue":"7","key":"ref44","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1038\/nsb0796-586","article-title":"Structural basis for specificity of Grb2-SH2 revealed by a novel ligand binding mode","volume":"3","author":"J Rahuel","year":"1996","journal-title":"Nat Struct Mol Biol"},{"issue":"5084","key":"ref45","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1126\/science.1279805","article-title":"Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein","volume":"258","author":"DJ Leahy","year":"1992","journal-title":"Science"},{"issue":"3","key":"ref46","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/S0969-2126(96)00036-6","article-title":"Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity","volume":"4","author":"S Improta","year":"1996","journal-title":"Structure"},{"issue":"5020","key":"ref47","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1126\/science.1871600","article-title":"A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G","volume":"253","author":"AM Gronenborn","year":"1991","journal-title":"Science"},{"issue":"3","key":"ref48","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/0022-2836(87)90679-6","article-title":"Structure of ubiquitin refined at 1.8 \u00c5 resolution","volume":"194","author":"S Vijay-Kumar","year":"1987","journal-title":"J Mol Biol"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"985","DOI":"10.1006\/jmbi.1998.1645","article-title":"Contact order, transition state placement and the refolding rates of single domain proteins","volume":"277","author":"KW Plaxco","year":"1998","journal-title":"J Mol Biol"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"11311","DOI":"10.1073\/pnas.96.20.11311","article-title":"A simple model for calculating the kinetics of protein folding from three-dimensional structures","volume":"96","author":"V Mu\u00f1oz","year":"1999","journal-title":"Proc Natl Acad Sci USA"},{"issue":"2","key":"ref51","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.chemphys.2004.06.064","article-title":"Combinatorial modeling of protein folding kinetics: free energy profiles and rates","volume":"307","author":"ER Henry","year":"2004","journal-title":"Chem Phys"},{"issue":"44","key":"ref52","doi-asserted-by":"crossref","first-page":"17880","DOI":"10.1073\/pnas.1317105110","article-title":"Comparing a simple theoretical model for protein folding with all-atom molecular dynamics simulations","volume":"110","author":"ER Henry","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1006\/jmbi.2000.3693","article-title":"Topological and energetic factors: what determines the structural details of the transition state ensemble and \u201cen-route\u201d intermediates for protein folding? An investigation for small globular proteins","volume":"298","author":"C Clementi","year":"2000","journal-title":"J Mol Biol"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"13235","DOI":"10.1021\/jp403305a","article-title":"How well does a funneled energy landscape capture the folding mechanism of spectrin domains","volume":"117","author":"RB Best","year":"2013","journal-title":"J Phys Chem B"},{"issue":"2","key":"ref55","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1073\/pnas.2534828100","article-title":"Protein topology determines binding mechanism","volume":"101","author":"Y Levy","year":"2004","journal-title":"Proc Natl Acad Sci USA"},{"issue":"4","key":"ref56","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1016\/j.jmb.2004.12.021","article-title":"A survey of flexible protein binding mechanisms and their transition states using native topology based energy landscapes","volume":"346","author":"Y Levy","year":"2005","journal-title":"J Mol Biol"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1016\/j.jmb.2004.12.021","article-title":"A survey of flexible protein binding mechanisms and their transition states using native topology based energy landscapes","volume":"346","author":"Y Levy","year":"2005","journal-title":"J Mol Biol"},{"issue":"1","key":"ref58","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.str.2005.09.008","article-title":"Topological determinants of protein domain swapping","volume":"14","author":"F Ding","year":"2006","journal-title":"Structure"},{"issue":"38","key":"ref59","doi-asserted-by":"crossref","first-page":"13786","DOI":"10.1073\/pnas.0403724101","article-title":"Domain swapping is a consequence of minimal frustration","volume":"101","author":"S Yang","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"S44","DOI":"10.1088\/1478-3975\/2\/2\/S05","article-title":"Overcoming residual frustration in domain-swapping: the roles of disulfide bonds in dimerization and aggregation","volume":"2","author":"SS Cho","year":"2005","journal-title":"Phys Biol"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.1021\/jp110738m","article-title":"Force-induced change in protein unfolding mechanism: discrete or continuous switch?","volume":"115","author":"TGW Graham","year":"2011","journal-title":"J Phys Chem B"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"208301","DOI":"10.1103\/PhysRevLett.107.208301","article-title":"Locating the folding barrier for single molecules under an external force","volume":"107","author":"OK Dudko","year":"2011","journal-title":"Phys Rev Lett"},{"issue":"4","key":"ref63","first-page":"637","article-title":"Sense and stretchability: The role of titin and titin-associated proteins in myocardial stress-sensing and mechanical dysfunction x2020;","volume":"77","author":"WA Linke","year":"2008","journal-title":"Cardiovascular Res"},{"key":"ref64","doi-asserted-by":"crossref","first-page":"1665","DOI":"10.1103\/PhysRevLett.67.1665","article-title":"Protein folding bottlenecks: a lattice Monte Carlo simulation","volume":"67","author":"E Shaknovich","year":"1991","journal-title":"Phys Rev Lett"},{"issue":"6","key":"ref65","doi-asserted-by":"crossref","first-page":"3995","DOI":"10.1529\/biophysj.104.042754","article-title":"Reversible mechanical unfolding of single ubiquitin molecules","volume":"87","author":"CL Chyan","year":"2004","journal-title":"Biophys J"},{"issue":"9","key":"ref66","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1038\/nsb965","article-title":"The mechanical stability of ubiquitin is linkage dependent","volume":"10","author":"M Carrion-Vazquez","year":"2003","journal-title":"Nat Struct Mol Biol"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1007\/s002140050198","article-title":"Kinetic partitioning mechanism as a unifying theme in the folding of biomolecules","volume":"96","author":"D Thirumalai","year":"1997","journal-title":"Theor Chem Acc"},{"issue":"9","key":"ref68","doi-asserted-by":"crossref","first-page":"2057","DOI":"10.1110\/ps.0302503","article-title":"Contact order revisited: influence of protein size on the folding rate","volume":"12","author":"DN Ivankov","year":"2003","journal-title":"Protein Sci"},{"issue":"9","key":"ref69","doi-asserted-by":"crossref","first-page":"1145","DOI":"10.1016\/S0969-2126(99)80181-6","article-title":"Folding studies of immunoglobulin-like <italic>\u03b2<\/italic>-sandwich proteins suggest that they share a common folding pathway","volume":"7","author":"J Clarke","year":"1999","journal-title":"Structure"},{"key":"ref70","article-title":"Tolerance of protein folding to a circular permutation in a PDZ domain","author":"G Hultqvist","year":"2012","journal-title":"PLoS Comput Biol"},{"issue":"2","key":"ref71","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1016\/j.bpc.2007.03.011","article-title":"Destabilised mutants of ubiquitin gain equal stability in crowded solutions","volume":"128","author":"A Roberts","year":"2007","journal-title":"Biophys Chem"},{"issue":"8","key":"ref72","doi-asserted-by":"crossref","first-page":"2053","DOI":"10.1016\/j.bpj.2011.09.013","article-title":"GB1 is not a two-state folder: identification and characterization of an on-pathway intermediate","volume":"101","author":"A Morrone","year":"2011","journal-title":"Biophys J"},{"key":"ref73","first-page":"1","article-title":"Markov State Models for Protein Misfolding","volume":"0","author":"A Sirur","year":"2016","journal-title":"J Chem Phys"},{"issue":"7","key":"ref74","doi-asserted-by":"crossref","first-page":"5006","DOI":"10.1039\/C4CP05203J","article-title":"Dimer domain swapping versus monomer folding in apo-myoglobin studied by molecular simulations","volume":"17","author":"K Ono","year":"2015","journal-title":"Phys Chem Chem Phys"},{"issue":"12","key":"ref75","doi-asserted-by":"crossref","first-page":"2780","DOI":"10.1002\/prot.24161","article-title":"Folding of multidomain proteins: Biophysical consequences of tethering even in apparently independent folding","volume":"80","author":"O Arviv","year":"2012","journal-title":"Proteins"},{"issue":"6","key":"ref76","doi-asserted-by":"crossref","first-page":"1939","DOI":"10.1143\/JPSJ.44.1939","article-title":"Statistical mechanical theory of the protein conformation. II. Folding pathway for protein","volume":"44","author":"H Wako","year":"1978","journal-title":"J Phys Soc Japan"},{"key":"ref77","doi-asserted-by":"crossref","first-page":"W232","DOI":"10.1093\/nar\/gks529","article-title":"CPred: a web server for predicting viable circular permutations in proteins","volume":"40","author":"WC Lo","year":"2012","journal-title":"Nucleic Acids Res"},{"key":"ref78","doi-asserted-by":"crossref","first-page":"2207","DOI":"10.1002\/pro.5560031206","article-title":"A revised set of potentials for <italic>\u03b2<\/italic>-turn formation","volume":"3","author":"EG Hutchinson","year":"1994","journal-title":"Protein Sci"}],"container-title":["PLOS Computational Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pcbi.1004933","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,6,21]],"date-time":"2022-06-21T03:22:58Z","timestamp":1655781778000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pcbi.1004933"}},"subtitle":[],"editor":[{"given":"Andrey","family":"Kajava","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2016,5,10]]},"references-count":78,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2016,5,10]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pcbi.1004933","relation":{},"ISSN":["1553-7358"],"issn-type":[{"value":"1553-7358","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,5,10]]}}}