Source:http://linkedlifedata.com/resource/pubmed/id/16206128
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
2006-3-15
|
pubmed:abstractText |
Based on the fiber diffraction data from native collagen, Rich and Crick proposed the 10/3-helical model with a 28.6 A axial repeat in 1955 (Rich A.; Crick, F. H. C. Nature (Lond) 1955, 176, 915-916). We obtained the 7/2-helical structure with a 20 A axial repeat from the single crystal analysis of (Pro-Pro-Gly)(10). Since the latter structure could explain fiber diffraction patterns from native collagen, we proposed this structure as a new model for collagen in 1977 (Okuyama et al., Polym J 1977, 9, 341-343). These two structural models were refined against observed continuous intensity data from native collagen using a linked-atom least-squares method. It was found that the diffraction data from native collagen could be explained by the 7/2-helical model better than, or at least the same as, the prevailing 10/3-helical model. Together with the evidence that recent single crystal analyses of many model peptides have supported the 7/2-helical model and there was no such active support for the 10/3-helical model, it was concluded that the average molecular structure of native collagen seems to be closer to the 7/2-helical symmetry than the other one.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:issn |
0006-3525
|
pubmed:author | |
pubmed:copyrightInfo |
Copyright 2005 Wiley Periodicals, Inc.
|
pubmed:issnType |
Print
|
pubmed:volume |
84
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
181-91
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:16206128-Animals,
pubmed-meshheading:16206128-Collagen,
pubmed-meshheading:16206128-Hydrogen Bonding,
pubmed-meshheading:16206128-Macropodidae,
pubmed-meshheading:16206128-Models, Molecular,
pubmed-meshheading:16206128-Peptides,
pubmed-meshheading:16206128-Protein Conformation,
pubmed-meshheading:16206128-Protein Structure, Secondary,
pubmed-meshheading:16206128-Tendons,
pubmed-meshheading:16206128-Water,
pubmed-meshheading:16206128-X-Ray Diffraction
|
pubmed:year |
2006
|
pubmed:articleTitle |
Revision of collagen molecular structure.
|
pubmed:affiliation |
Faculty of Technology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan. okuyamak@chem.sci.osaka-u.ac.jp
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|