{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,7]],"date-time":"2026-04-07T01:30:18Z","timestamp":1775525418363,"version":"3.50.1"},"reference-count":58,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2011,7,1]],"date-time":"2011-07-01T00:00:00Z","timestamp":1309478400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,7,16]],"date-time":"2013-07-16T00:00:00Z","timestamp":1373932800000},"content-version":"vor","delay-in-days":746,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biophysical Journal"],"published-print":{"date-parts":[[2011,7]]},"DOI":"10.1016\/j.bpj.2011.06.017","type":"journal-article","created":{"date-parts":[[2011,7,23]],"date-time":"2011-07-23T23:19:46Z","timestamp":1311463186000},"page":"449-458","source":"Crossref","is-referenced-by-count":29,"title":["Osteogenesis Imperfecta Model Peptides: Incorporation of Residues Replacing Gly within a Triple Helix Achieved by Renucleation and Local Flexibility"],"prefix":"10.1016","volume":"101","author":[{"given":"Jianxi","family":"Xiao","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Balaraman","family":"Madhan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yingjie","family":"Li","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Barbara","family":"Brodsky","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jean","family":"Baum","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bpj.2011.06.017_bib1","doi-asserted-by":"crossref","first-page":"7","DOI":"10.3109\/07853890109002055","article-title":"Collagens and collagen-related diseases","volume":"33","author":"Myllyharju","year":"2001","journal-title":"Ann. Med."},{"key":"10.1016\/j.bpj.2011.06.017_bib2","series-title":"Connective Tissue and Its Hereditable Disorders: Molecular, Genetic, and Medical Aspects","first-page":"385","article-title":"Osteogenesis imperfecta","author":"Byers","year":"2002"},{"key":"10.1016\/j.bpj.2011.06.017_bib3","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1002\/humu.20429","article-title":"Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans","volume":"28","author":"Marini","year":"2007","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.bpj.2011.06.017_bib4","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1146\/annurev.biochem.77.032207.120833","article-title":"Collagen structure and stability","volume":"78","author":"Shoulders","year":"2009","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bpj.2011.06.017_bib5","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1038\/176593a0","article-title":"Structure of collagen","volume":"176","author":"Ramachandran","year":"1955","journal-title":"Nature"},{"key":"10.1016\/j.bpj.2011.06.017_bib6","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1038\/176915a0","article-title":"The structure of collagen","volume":"176","author":"Rich","year":"1955","journal-title":"Nature"},{"key":"10.1016\/j.bpj.2011.06.017_bib7","series-title":"Connective Tissue and Its Heritable Disorders: Molecular, Genetic, and Medical Aspects","first-page":"159","article-title":"The collagen family: strucutre, assembly, and organization in the extracellular matrix","author":"Kielty","year":"2002"},{"key":"10.1016\/j.bpj.2011.06.017_bib8","doi-asserted-by":"crossref","first-page":"820","DOI":"10.1042\/bst0190820","article-title":"Structure and function of the fibril-associated collagens","volume":"19","author":"van der Rest","year":"1991","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.bpj.2011.06.017_bib9","unstructured":"Dalgleish, R. Osteogenesis imperfecta and Ehlers-Danlos syndrome variant databases. Leiden University Medical Center, Leiden, The Netherlands. http:\/\/www.le.ac.uk\/genetics\/collagen\/."},{"key":"10.1016\/j.bpj.2011.06.017_bib10","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1038\/316363a0","article-title":"Subtle structural alterations in the chains of type I procollagen produce osteogenesis imperfecta type II","volume":"316","author":"Bonadio","year":"1985","journal-title":"Nature"},{"key":"10.1016\/j.bpj.2011.06.017_bib11","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1016\/j.matbio.2007.06.005","article-title":"Selective retention and degradation of molecules with a single mutant \u03b11(I) chain in the Brtl IV mouse model of OI","volume":"26","author":"Forlino","year":"2007","journal-title":"Matrix Biol."},{"key":"10.1016\/j.bpj.2011.06.017_bib12","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.tcb.2010.11.007","article-title":"Chaperoning osteogenesis: new protein-folding disease paradigms","volume":"21","author":"Makareeva","year":"2011","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.bpj.2011.06.017_bib13","doi-asserted-by":"crossref","first-page":"4223","DOI":"10.1074\/jbc.M110709200","article-title":"Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen","volume":"277","author":"Di Lullo","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2011.06.017_bib14","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1016\/S0959-440X(99)80016-5","article-title":"Folding of peptide models of collagen and misfolding in disease","volume":"9","author":"Baum","year":"1999","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bpj.2011.06.017_bib15","doi-asserted-by":"crossref","first-page":"4787","DOI":"10.1074\/jbc.M705773200","article-title":"Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta","volume":"283","author":"Makareeva","year":"2008","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2011.06.017_bib16","doi-asserted-by":"crossref","first-page":"34337","DOI":"10.1074\/jbc.M805485200","article-title":"Recombinant collagen studies link the severe conformational changes induced by osteogenesis imperfecta mutations to the disruption of a set of interchain salt bridges","volume":"283","author":"Xu","year":"2008","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2011.06.017_bib17","doi-asserted-by":"crossref","first-page":"20660","DOI":"10.1074\/jbc.M109.018077","article-title":"NMR conformational and dynamic consequences of a gly to ser substitution in an osteogenesis imperfecta collagen model peptide","volume":"284","author":"Li","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2011.06.017_bib18","doi-asserted-by":"crossref","first-page":"5424","DOI":"10.1021\/bi800026k","article-title":"Predicting the clinical lethality of osteogenesis imperfecta from collagen glycine mutations","volume":"47","author":"Bodian","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2011.06.017_bib19","doi-asserted-by":"crossref","first-page":"5314","DOI":"10.1021\/bi035676w","article-title":"Severity of osteogenesis imperfecta and structure of a collagen-like peptide modeling a lethal mutation site","volume":"43","author":"Radmer","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2011.06.017_bib20","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1002\/humu.20091","article-title":"Stability related bias in residues replacing glycines within the collagen triple helix (Gly-Xaa-Yaa) in inherited connective tissue disorders","volume":"24","author":"Persikov","year":"2004","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.bpj.2011.06.017_bib21","doi-asserted-by":"crossref","first-page":"4273","DOI":"10.1073\/pnas.070050097","article-title":"Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine","volume":"97","author":"Beck","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2011.06.017_bib22","doi-asserted-by":"crossref","first-page":"34181","DOI":"10.1074\/jbc.M110.128355","article-title":"Local conformation and dynamics of isoleucine in the collagenase cleavage site provide a recognition signal for matrix metalloproteinases","volume":"285","author":"Xiao","year":"2010","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2011.06.017_bib23","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1002\/bip.20958","article-title":"Triple-helical peptides: an approach to collagen conformation, stability, and self-association","volume":"89","author":"Brodsky","year":"2008","journal-title":"Biopolymers"},{"key":"10.1016\/j.bpj.2011.06.017_bib24","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1126\/science.7695699","article-title":"Crystal and molecular structure of a collagen-like peptide at 1.9\u00a0\u00c5 resolution","volume":"266","author":"Bella","year":"1994","journal-title":"Science"},{"key":"10.1016\/j.bpj.2011.06.017_bib25","doi-asserted-by":"crossref","first-page":"10490","DOI":"10.1021\/ja052801d","article-title":"Identification of partially disordered peptide intermediates through residue-specific NMR diffusion measurements","volume":"127","author":"Li","year":"2005","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2011.06.017_bib26","doi-asserted-by":"crossref","first-page":"13520","DOI":"10.1021\/ja805496v","article-title":"NMR monitoring of chain-specific stability in heterotrimeric collagen peptides","volume":"130","author":"Madhan","year":"2008","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2011.06.017_bib27","doi-asserted-by":"crossref","first-page":"7377","DOI":"10.1021\/bi00080a007","article-title":"Two-dimensional NMR assignments and conformation of (Pro-Hyp-Gly)10 and a designed collagen triple-helical peptide","volume":"32","author":"Li","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2011.06.017_bib28","doi-asserted-by":"crossref","first-page":"18194","DOI":"10.1021\/ja9056823","article-title":"Structural insights from 15N relaxation data for an anisotropic collagen peptide","volume":"131","author":"Xiao","year":"2009","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2011.06.017_bib29","doi-asserted-by":"crossref","first-page":"22699","DOI":"10.1074\/jbc.M702910200","article-title":"NMR shows hydrophobic interactions replace glycine packing in the triple helix at a natural break in the (Gly-X-Y)n repeat","volume":"282","author":"Li","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2011.06.017_bib30","first-page":"337a","article-title":"Collagen model peptides: support for an internal nucleation site in type I collagen","volume":"84","author":"Bryan","year":"2003","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2011.06.017_bib31","doi-asserted-by":"crossref","first-page":"13299","DOI":"10.1021\/bi00211a043","article-title":"Backbone dynamics of (Pro-Hyp-Gly)10 and a designed collagen-like triple-helical peptide by 15N NMR relaxation and hydrogen-exchange measurements","volume":"32","author":"Fan","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2011.06.017_bib32","doi-asserted-by":"crossref","first-page":"15528","DOI":"10.1021\/bi981147u","article-title":"Nuclear magnetic resonance shows asymmetric loss of triple helix in peptides modeling a collagen mutation in brittle bone disease","volume":"37","author":"Liu","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2011.06.017_bib33","doi-asserted-by":"crossref","first-page":"36937","DOI":"10.1074\/jbc.M605135200","article-title":"Sequence dependence of renucleation after a Gly mutation in model collagen peptides","volume":"281","author":"Hyde","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2011.06.017_bib34","doi-asserted-by":"crossref","first-page":"6539","DOI":"10.1021\/bi020070d","article-title":"Folding and conformational consequences of glycine to alanine replacements at different positions in a collagen model peptide","volume":"41","author":"Bhate","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2011.06.017_bib35","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1002\/bip.21432","article-title":"Sequence environment of mutation affects stability and folding in collagen model peptides of osteogenesis imperfecta","volume":"96","author":"Bryan","year":"2011","journal-title":"Biopolymers"},{"key":"10.1016\/j.bpj.2011.06.017_bib36","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1110\/ps.03501704","article-title":"Equilibrium thermal transitions of collagen model peptides","volume":"13","author":"Persikov","year":"2004","journal-title":"Protein Sci."},{"key":"10.1016\/j.bpj.2011.06.017_bib37","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1021\/j100624a025","article-title":"Self-diffusion in normal and heavy water in the range 1\u201345\u00b0","volume":"77","author":"Mills","year":"1973","journal-title":"J.\u00a0Phys. Chem."},{"key":"10.1016\/j.bpj.2011.06.017_bib38","first-page":"115","article-title":"Calibration in accurate spin-echo self-diffusion measurements using 1H and less-common nuclei","volume":"92","author":"Holz","year":"1991","journal-title":"J.\u00a0Magn. Reson."},{"key":"10.1016\/j.bpj.2011.06.017_bib39","doi-asserted-by":"crossref","first-page":"1991","DOI":"10.1021\/jp9842953","article-title":"Thermal offset viscosities of liquid H2O, D2O, and T2O","volume":"103","author":"Cho","year":"1999","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.bpj.2011.06.017_bib40","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1006\/jmbi.2001.5328","article-title":"Distribution of molecular size within an unfolded state ensemble using small-angle x-ray scattering and pulse field gradient NMR techniques","volume":"316","author":"Choy","year":"2002","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.bpj.2011.06.017_bib41","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1006\/jmre.2000.2158","article-title":"Cross-relaxation effects in stimulated-echo-type PGSE NMR experiments by bipolar and monopolar gradient pulses","volume":"146","author":"Dvinskikh","year":"2000","journal-title":"J.\u00a0Magn. Reson."},{"key":"10.1016\/j.bpj.2011.06.017_bib42","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1080\/07391102.1999.10508348","article-title":"Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-diffusion measurements","volume":"17","author":"Orekhov","year":"1999","journal-title":"J.\u00a0Biomol. Struct. Dyn."},{"key":"10.1016\/j.bpj.2011.06.017_bib43","doi-asserted-by":"crossref","first-page":"9094","DOI":"10.1021\/ja9809410","article-title":"Chemical exchange in diffusion NMR experiments","volume":"120","author":"Chen","year":"1998","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2011.06.017_bib44","doi-asserted-by":"crossref","first-page":"S98","DOI":"10.1002\/mrc.1124","article-title":"F-19 diffusion NMR analysis of enzyme-inhibitor binding","volume":"40","author":"Derrick","year":"2002","journal-title":"Magn. Reson. Chem."},{"key":"10.1016\/j.bpj.2011.06.017_bib45","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1006\/jmre.1998.1472","article-title":"Practical aspects of the measurement of the diffusion of proteins in aqueous solution","volume":"133","author":"Tillett","year":"1998","journal-title":"J.\u00a0Magn. Reson."},{"key":"10.1016\/j.bpj.2011.06.017_bib46","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1023\/B:JNMR.0000032560.43738.6a","article-title":"Characterization of phospholipid mixed micelles by translational diffusion","volume":"29","author":"Chou","year":"2004","journal-title":"J.\u00a0Biomol. NMR"},{"key":"10.1016\/j.bpj.2011.06.017_bib47","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1002\/prot.340170110","article-title":"Primary structure effects on peptide group hydrogen exchange","volume":"17","author":"Bai","year":"1993","journal-title":"Proteins"},{"key":"10.1016\/j.bpj.2011.06.017_bib48","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1023\/A:1008276004875","article-title":"Accurate quantitation of water-amide proton exchange rates using the phase-modulated CLEAN chemical EXchange (CLEANEX-PM) approach with a Fast-HSQC (FHSQC) detection scheme","volume":"11","author":"Hwang","year":"1998","journal-title":"J.\u00a0Biomol. NMR"},{"key":"10.1016\/j.bpj.2011.06.017_bib49","doi-asserted-by":"crossref","first-page":"4299","DOI":"10.1021\/bi992584r","article-title":"Site-specific NMR monitoring of cis-trans isomerization in the folding of the proline-rich collagen triple helix","volume":"39","author":"Buevich","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2011.06.017_bib50","doi-asserted-by":"crossref","first-page":"7156","DOI":"10.1021\/ja012699u","article-title":"Residue-specific real-time NMR diffusion experiments define the association states of proteins during folding","volume":"124","author":"Buevich","year":"2002","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2011.06.017_bib51","doi-asserted-by":"crossref","first-page":"46890","DOI":"10.1074\/jbc.M407061200","article-title":"Transformation of the mechanism of triple-helix peptide folding in the absence of a C-terminal nucleation domain and its implications for mutations in collagen disorders","volume":"279","author":"Buevich","year":"2004","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2011.06.017_bib52","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1042\/bj0740238","article-title":"Structural changes in collagen. The action of alkalis and acids in the conversion of collagen into eucollagen","volume":"74","author":"Courts","year":"1960","journal-title":"Biochem.\u00a0J."},{"key":"10.1016\/j.bpj.2011.06.017_bib53","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1042\/bj0430365","article-title":"The effect of alkalis on collagen","volume":"43","author":"Bowes","year":"1948","journal-title":"Biochem.\u00a0J."},{"key":"10.1016\/j.bpj.2011.06.017_bib54","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1002\/1097-0282(200103)58:3<347::AID-BIP1011>3.0.CO;2-M","article-title":"Computed free energy differences between point mutations in a collagen-like peptide","volume":"58","author":"Mooney","year":"2001","journal-title":"Biopolymers"},{"key":"10.1016\/j.bpj.2011.06.017_bib55","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1146\/annurev.bb.20.060191.001033","article-title":"The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper","volume":"20","author":"Engel","year":"1991","journal-title":"Annu. Rev. Biophys. Biophys. Chem."},{"key":"10.1016\/j.bpj.2011.06.017_bib56","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1006\/jmbi.1994.1199","article-title":"Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta","volume":"236","author":"Raghunath","year":"1994","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.bpj.2011.06.017_bib57","doi-asserted-by":"crossref","first-page":"7509","DOI":"10.1021\/ja801670v","article-title":"Synthetic collagen heterotrimers: structural mimics of wild-type and mutant collagen type I","volume":"130","author":"Gauba","year":"2008","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2011.06.017_bib58","doi-asserted-by":"crossref","first-page":"2041","DOI":"10.1074\/jbc.M110.153965","article-title":"Location of glycine mutations within a bacterial collagen protein affects degree of disruption of triple-helix folding and conformation","volume":"286","author":"Cheng","year":"2011","journal-title":"J.\u00a0Biol. Chem."}],"container-title":["Biophysical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349511007144?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349511007144?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,12,1]],"date-time":"2018-12-01T10:30:31Z","timestamp":1543660231000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006349511007144"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,7]]},"references-count":58,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2011,7]]}},"alternative-id":["S0006349511007144"],"URL":"https:\/\/doi.org\/10.1016\/j.bpj.2011.06.017","relation":{},"ISSN":["0006-3495"],"issn-type":[{"value":"0006-3495","type":"print"}],"subject":[],"published":{"date-parts":[[2011,7]]}}}