{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T20:37:26Z","timestamp":1788554246456,"version":"build-2803163510"},"reference-count":50,"publisher":"American Chemical Society (ACS)","issue":"20","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochemistry"],"published-print":{"date-parts":[[2002,5,1]]},"DOI":"10.1021\/bi020070d","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T06:09:00Z","timestamp":1027663740000},"page":"6539-6547","source":"Crossref","is-referenced-by-count":38,"title":["Folding and Conformational Consequences of Glycine to Alanine Replacements at Different Positions in a Collagen Model Peptide"],"prefix":"10.1021","volume":"41","author":[{"given":"Manjiri","family":"Bhate","sequence":"first","affiliation":[{"name":"Department of Biochemistry, UMDNJ\u2212Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, New Jersey 08854, and Department of Chemistry, Rutgers University, Piscataway, New Jersey 08854"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xin","family":"Wang","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, UMDNJ\u2212Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, New Jersey 08854, and Department of Chemistry, Rutgers University, Piscataway, New Jersey 08854"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean","family":"Baum","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, UMDNJ\u2212Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, New Jersey 08854, and Department of Chemistry, Rutgers University, Piscataway, New Jersey 08854"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Barbara","family":"Brodsky","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, UMDNJ\u2212Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, New Jersey 08854, and Department of Chemistry, Rutgers University, Piscataway, New Jersey 08854"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2002,4,26]]},"reference":[{"key":"bi020070db00001\/bi020070db00001_1","doi-asserted-by":"crossref","first-page":"21","DOI":"10.3109\/07853890109002055","volume":"33","author":"Myllyharju J.","year":"2001","journal-title":"Ann. Med."},{"key":"bi020070db00002\/bi020070db00002_1","volume-title":"II, III and XI), fibril-associated collagen (type IX) and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels. Hum. Mutat. 9, 300\u2212315.","author":"Kuivaniemi H.","year":"1997"},{"key":"bi020070db00003\/bi020070db00003_1","volume-title":"Connective Tissue and its Hereditable Disorders:\u2009 Molecular, Genetic and Medical Aspects","author":"Byers P. H.","year":"1993"},{"key":"bi020070db00004\/bi020070db00004_1","doi-asserted-by":"crossref","DOI":"10.1016\/S0923-1811(99)00018-3","volume":"20","author":"Bruckner-Tuderman L.","year":"1999","journal-title":"J. Dermatol. Sci."},{"key":"bi020070db00005\/bi020070db00005_1","volume-title":"Proc. Natl. Acad. Sci. U.S.A. 98","author":"Camacho Vanegas O.","year":"2001"},{"key":"bi020070db00006\/bi020070db00006_1","doi-asserted-by":"crossref","DOI":"10.1098\/rstb.2000.0760","volume":"356","author":"Byers P. H.","year":"2001","journal-title":"Philos. Trans. R. Soc. London, Ser. B"},{"key":"bi020070db00007\/bi020070db00007_1","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1038\/ng0995-87","volume":"11","author":"Tiller G. E.","year":"1995","journal-title":"Nat. Genet."},{"key":"bi020070db00008\/bi020070db00008_1","volume-title":"The clinical spectrum of type IV collagen mutations. Hum. Mutat. 9, 477\u2212499","author":"Lemmink H. H.","year":"1997"},{"key":"bi020070db00009\/bi020070db00009_1","volume-title":"Subtle structural alterations in the chains of type I procollagen produce osteogenesis imperfecta type II. Nature 316, 363\u2212366","author":"Bonadio J.","year":"1985"},{"key":"bi020070db00010\/bi020070db00010_1","doi-asserted-by":"crossref","DOI":"10.1006\/jmbi.1994.1199","volume":"236","author":"Raghunath M.","year":"1994","journal-title":"J. Mol. Biol."},{"key":"bi020070db00011\/bi020070db00011_1","doi-asserted-by":"crossref","DOI":"10.1002\/ajmg.1320450204","volume":"45","author":"Bachinger H. P.","year":"1993","journal-title":"Am. J. Med. Genet."},{"key":"bi020070db00012\/bi020070db00012_1","volume-title":"Folding of peptide models of collagen and misfolding in disease. Curr. Opin. Struct. Biol. 9, 122\u2212128","author":"Baum J.","year":"1999"},{"key":"bi020070db00013\/bi020070db00013_1","first-page":"351","volume-title":"Mechanisms of Protein Folding","author":"Baum J.","year":"2000"},{"key":"bi020070db00014\/bi020070db00014_1","volume-title":"Connective Tissue and its Hereditable Disorders:\u2009 Molecular, Genetic, and Medical Apsects","author":"Kielty C. M.","year":"1993"},{"key":"bi020070db00015\/bi020070db00015_1","volume-title":"Collectin structure:\u2009 a review. Protein Sci. 9, 1607\u22121617","author":"Hakansson K.","year":"2000"},{"key":"bi020070db00016\/bi020070db00016_1","first-page":"183","volume-title":"Treatise on Collagen","author":"Ramachandran G. N.","year":"1964"},{"key":"bi020070db00017\/bi020070db00017_1","volume":"3","author":"Rich A.","year":"1961","journal-title":"J. Mol. Biol."},{"key":"bi020070db00018\/bi020070db00018_1","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1126\/science.7695699","volume":"266","author":"Bella J.","year":"1994","journal-title":"Science"},{"key":"bi020070db00019\/bi020070db00019_1","volume":"303","author":"Sakikabara S.","year":"1973","journal-title":"Biochim. Biophys. Acta"},{"key":"bi020070db00020\/bi020070db00020_1","volume-title":"The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen. Biochem. Biophys. Res. Commun. 52, 115\u2212120","author":"Berg R. A.","year":"1973"},{"key":"bi020070db00021\/bi020070db00021_1","volume-title":"New analysis of the phylogenetic change of collagen thermostability. Biopolymers 53, 523\u2212528","author":"Burjanadze T. V.","year":"2000"},{"key":"bi020070db00022\/bi020070db00022_1","first-page":"104","volume":"35","author":"Privalov P.","year":"1982","journal-title":"Adv. Protein Chem."},{"key":"bi020070db00023\/bi020070db00023_1","doi-asserted-by":"crossref","DOI":"10.1021\/ja005542v","volume":"123","author":"Bretscher L. E.","year":"2001","journal-title":"J. Am. Chem. Soc."},{"key":"bi020070db00024\/bi020070db00024_1","volume-title":"Preferred proline puckerings in cis and trans peptide groups:\u2009 Implications for collagen stability. Protein Sci. 10, 2627\u22122632","author":"Vitagliano L.","year":"2001"},{"key":"bi020070db00025\/bi020070db00025_1","volume-title":"The renaturation of soluble collagen. Products formed at different temperatures. Biochemistry 5, 2744\u22122755","author":"Beier G.","year":"1966"},{"key":"bi020070db00026\/bi020070db00026_1","volume-title":"Collagen structure in solution. II. Analysis of refolding kinetics in terms of nucleation and growth processes. Biochemistry 9, 3725\u22123733","author":"Harrington W. F.","year":"1970"},{"key":"bi020070db00027\/bi020070db00027_1","volume-title":"Molecular recognition in procollagen chain assembly. Matrix Biol. 16, 369\u2212377","author":"McLaughlin S. H.","year":"1998"},{"key":"bi020070db00028\/bi020070db00028_1","volume-title":"Procollagen folding and assembly:\u2009 The role of endoplasmic reticulum enzymes and molecular chaperones. Cell Dev. Biol. 10, 455\u2212464","author":"Lamande S. R.","year":"1999"},{"key":"bi020070db00029\/bi020070db00029_1","doi-asserted-by":"crossref","DOI":"10.1093\/emboj\/16.22.6694","volume":"16","author":"Bulleid N. J.","year":"1997","journal-title":"EMBO J."},{"key":"bi020070db00030\/bi020070db00030_1","doi-asserted-by":"crossref","DOI":"10.1111\/j.1432-1033.1978.tb12641.x","volume":"90","author":"Bachinger H. P.","year":"1978","journal-title":"Eur. J. Biochem."},{"key":"bi020070db00031\/bi020070db00031_1","doi-asserted-by":"crossref","DOI":"10.1111\/j.1432-1033.1980.tb04610.x","volume":"106","author":"Bachinger H. P.","year":"1980","journal-title":"Eur. J. Biochem."},{"key":"bi020070db00032\/bi020070db00032_1","volume-title":"Perspectives on synthesis and applications of triple-helical collagen model peptides. Biopolymers 40, 345\u2212357","author":"Fields G. B.","year":"1996"},{"key":"bi020070db00033\/bi020070db00033_1","volume-title":"Collagen mimetics. Biopolymers 47, 127\u2212142","author":"Goodman M.","year":"1998"},{"key":"bi020070db00034\/bi020070db00034_1","volume-title":"Amino acid sequence modulates the disruption by osteogenesis imperfecta glycine substitutions in collagen-like peptides. Biochemistry 36, 6930\u22126935","author":"Yang W.","year":"1997"},{"key":"bi020070db00035\/bi020070db00035_1","volume-title":"NMR shows asymmetric loss of triple-helix in peptides modeling a collagen mutation in brittle bone disease. Biochemistry 37, 15528\u221215533","author":"Liu X.","year":"1998"},{"key":"bi020070db00036\/bi020070db00036_1","volume-title":"Site specific NMR monitoring of cis\u2212trans isomerization in the folding of the proline-rich collagen triple-helix. Biochemistry 39, 4299\u22124308","author":"Buevich A. V.","year":"2000"},{"key":"bi020070db00037\/bi020070db00037_1","volume":"268","author":"Marini J. C.","year":"1993","journal-title":"J. Biol. Chem."},{"key":"bi020070db00039\/bi020070db00039_1","volume-title":"Mild dominant osteogenesis imperfecta with intrafamilial variability:\u2009 the cause is a serine for glycine alpha 1(I) 901 substitution in a type-I collagen gene. Hum. Genet. 89, 480\u2212484","author":"Mottes M.","year":"1992"},{"key":"bi020070db00040\/bi020070db00040_1","volume-title":"Characterization of collagen-like peptides containing interruptions in the repeating Gly-X-Y sequence. Biochemistry 32, 11688\u221211695","author":"Long C. G.","year":"1993"},{"key":"bi020070db00041\/bi020070db00041_1","volume-title":"Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. Biochemistry 33, 5984\u22126003","author":"Farrow N. A.","year":"1994"},{"key":"bi020070db00042\/bi020070db00042_1","volume-title":"Thermodynamic Analysis of a designed three-stranded coiled coil. Biochemistry 35, 14480\u221214485","author":"Boice J. A.","year":"1996"},{"key":"bi020070db00043\/bi020070db00043_1","volume-title":"Conformational Change of the Triple-Helical Structure. III. Stabilizing forces in the triple-helix. Biopolymers 13, 2461\u22122475","author":"Sutoh K.","year":"1974"},{"key":"bi020070db00044\/bi020070db00044_1","unstructured":"Li, M.H. (1993) NMR Studies of Triple-helical Peptides. Ph.D. Thesis, Rutgers University."},{"key":"bi020070db00045\/bi020070db00045_1","volume-title":"Proc. Natl. Acad. Sci. U.S.A. 93","author":"Beck K.","year":"2000"},{"key":"bi020070db00046\/bi020070db00046_1","doi-asserted-by":"crossref","DOI":"10.1098\/rstb.2000.0761","volume":"356","author":"Buevich A.","year":"2001","journal-title":"Philos. Trans. R. Soc. London, Ser. B"},{"key":"bi020070db00047\/bi020070db00047_1","volume-title":"Computational investigations of structural changes resulting from point mutations in a collagen-like peptide. Biopolymers 49, 167\u2212183","author":"Klein T. E.","year":"1999"},{"key":"bi020070db00048\/bi020070db00048_1","doi-asserted-by":"crossref","DOI":"10.1016\/S0022-2836(64)80207-2","volume":"9","author":"Josse J.","year":"1964","journal-title":"J. Mol. Biol."},{"key":"bi020070db00049\/bi020070db00049_1","volume-title":"Equilibrium and kinetic studies of the helix-coil transition in \u03b11-CB2, a small peptide from collagen. Biochemistry 9, 4134\u22124140","author":"Piez K. A.","year":"1970"},{"key":"bi020070db00050\/bi020070db00050_1","doi-asserted-by":"crossref","DOI":"10.1016\/S0021-9258(18)52286-9","volume":"266","author":"Wenstrup R. J.","year":"1991","journal-title":"J. Biol. Chem."},{"key":"bi020070dn00001\/bi020070dn00001_1","volume-title":"circular dichroism","author":"Abbreviations CD"}],"container-title":["Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/bi020070d","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,9,20]],"date-time":"2021-09-20T02:49:55Z","timestamp":1632106195000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/doi\/10.1021\/bi020070d"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,4,26]]},"references-count":50,"journal-issue":{"issue":"20","published-print":{"date-parts":[[2002,5,1]]}},"alternative-id":["10.1021\/bi020070d"],"URL":"https:\/\/doi.org\/10.1021\/bi020070d","relation":{},"ISSN":["0006-2960","1520-4995"],"issn-type":[{"value":"0006-2960","type":"print"},{"value":"1520-4995","type":"electronic"}],"subject":[],"published":{"date-parts":[[2002,4,26]]}}}