SOLUBLE FRAGMENTS OF ELASTIN. CIRCULAR DICHROISM STUDIES
- 1 March 1973
- journal article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 5 (2) , 63-68
- https://doi.org/10.1111/j.1399-3011.1973.tb02319.x
Abstract
Using alcoholic KOH, elastin has been hydrolyzed and two homogeneous fragments have been isolated by Amberlite IR‐120 chromatography. The peptides have been studied by circular dichroism in different solvents and in presence of Ca++ ions. The results are discussed from the standpoint of the free conformation in solution and the Ca++ ions complexation.Keywords
This publication has 15 references indexed in Scilit:
- Calcium ion effects a notable change in elastin conformation by interacting at neutral sitesBiochemical and Biophysical Research Communications, 1971
- Circular dichroism of cyclic hexapeptides with one and two side chainsBiochemistry, 1971
- Neutral Sites for Calcium Ion Binding to Elastin and Collagen: A Charge Neutralization Theory for Calcification and Its Relationship to AtherosclerosisProceedings of the National Academy of Sciences, 1971
- Comparison of Soluble and Native Elastin Conformations by Far-ultraviolet Circular DichroismNature, 1970
- Coacervation of Solubilized Elastin effects a Notable Conformational ChangeNature, 1969
- Evidence for Order in the Structure of α-ElastinNature, 1968
- Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide unitsBiopolymers, 1968
- Ultraviolet rotatory properties of polypeptides in solution. I. Helical poly-L-alanineJournal of the American Chemical Society, 1968
- “Cross-β” conformation in proteinsJournal of Molecular Biology, 1968
- Determination of the N-terminal Amino-acid in Polypeptides and ProteinsNature, 1965