Interchain Interactions in Collagen-Fold Formation. I. The Kinetics of Renaturation of γ-Gelatin*
- 1 February 1964
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 3 (2) , 135-145
- https://doi.org/10.1021/bi00890a001
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- The characterization of the γ-component of gelatinArchives of Biochemistry and Biophysics, 1962
- Investigation of the denaturation and renaturation of soluble collagen by light scatteringArchives of Biochemistry and Biophysics, 1962
- GAMMA TROPOCOLLAGEN: A REVERSIBLY DENATURABLE COLLAGEN MACROMOLECULEProceedings of the National Academy of Sciences, 1961
- The long range reorganization of gelatin to the collagen structureArchives of Biochemistry and Biophysics, 1961
- The molecular structure of polyadenylic acidJournal of Molecular Biology, 1961
- SEPARATION AND CHARACTERIZATION OF THE ALPHA-COMPONENTS AND BETA-COMPONENTS OF CALF SKIN COLLAGEN1960
- Enzymic studies of the gelatin → collagen-fold transitionBiochimica et Biophysica Acta, 1959
- Two Tripeptides from an Enzymatic Digest of CollagenJournal of Biological Chemistry, 1959
- Studies on the structure of poly-l-proline in solutionBiochimica et Biophysica Acta, 1958
- Peptides Isolated from a Partial Hydrolysate of Steer Hide Collagen. II. Evidence for the Prolyl-Hydroxyproline Linkage in CollagenJournal of the American Chemical Society, 1955