1.
Biofizika
; 32(2): 226-8, 1987.
Article
in Russian
| MEDLINE
| ID: mdl-3580391
ABSTRACT
Conformation structure of soluble collagen in anhydrous form, films and gels was studied by broad line NMR. An analysis of spectra points to partial ordering of polymer chains in the films and possible formation of secondary structure of collagen molecules by alpha-helix type. Distinction of gel spectra from those of films is explained by unordered rotation movements of the chain fragments at the expense of "superspiralization" of collagen molecules.
Subject(s)
Collagen , Magnetic Resonance Spectroscopy , Protein Conformation , Solubility
2.
Farmatsiia
; 25(4): 21-3, 1976.
Article
in Russian
| MEDLINE
| ID: mdl-1010045
3.
Farmatsiia
; 25(3): 18-21, 1976.
Article
in Russian
| MEDLINE
| ID: mdl-950028