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Molecular dynamics of collagen side chains in hard and soft tissues. A multinuclear magnetic resonance study

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00395a032· OSTI ID:5513063
The authors have prepared samples of (a) intact calvaria collagen (cross-linked and mineralized), (b) intact tendon collagen (cross-linked but not mineralized), and (c) reconstituted chick calvaria collagen (not cross-linked and not mineralized) containing (methyl-/sup 2/H/sub 3/)methionyl, (4,4-/sup 2/H/sub 2/)pyrrolidinyl, (4-fluorophenyl)alanyl, and (6-/sup 15/N)lysyl residues.Using multinuclear magnetic resonance spectroscopy, they have investigated the molecular dynamics of the labeled amino acids. Guided by model compound studies, they reached the following conclusions regarding collagen side chain dynamics from their analysis of line shapes and relaxation rates. At 22/sup 0/C, imino residues in all samples have flexible rings with root mean square angular fluctuations in the 11-30/sup 0/ range. Nearly all labeled amino acid side chains reorient about at least two side chain single bonds. At temperatures below -30/sup 0/C, most of these side chain motions are absent in all the samples. Surprisingly, in contrast with results obtained for backbone motions, side chain motions are only marginally more hindered in mineralized samples as compared with nonmineralized samples, a result they discuss with reference to collagen-mineral interactions. They also discuss the possible relationship between collagen dynamics and function.
Research Organization:
National Institutes of Health, Bethesda, MD
OSTI ID:
5513063
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 26:21; ISSN BICHA
Country of Publication:
United States
Language:
English