The triple helix-coil transition of cyanogen-bromide peptides of the ?1-chain of the calf-skin collagen
Author:
Publisher
Wiley
Subject
Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics
Reference15 articles.
1. (1967) in Treatise in Collagen, Vol. 1, Ed., Academic, New York, pp. 253-338.
2. Thermal conformational transformation of tropocollagen. I. Calorimetric study
3. The association reaction of collagen model polypeptides (Pro-Pro-Gly)n
4. The triple helix ? coil conversion of collagen-like polytripeptides in aqueous and nonaqueous solvents. Comparison of the thermodynamic parameters and the binding of water to (L-Pro-L-Pro-Gly)n and (L-Pro-L-Hyp-Gly)n
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1. TRIPLE HELIX COIL TRANSITION OF A BLOCKPOLYMER WITH THE SEQUENCE BOC-(GLY-PRO-PRO)5-(GLY-PRO-LEU)5-(GLY-PRO-PRO)5-NH2;International Journal of Peptide and Protein Research;2009-01-12
2. Equilibrium thermal transitions of collagen model peptides;Protein Science;2004-04-01
3. Properties of thermoreversible gels;Berichte der Bunsengesellschaft für physikalische Chemie;1998-11
4. Stability of type I collagen CNBr peptide trimers;Journal of Molecular Biology;1997-06
5. Type I Collagen CNBr Peptides: Species and Behavior in Solution;Biochemistry;1996-01-01
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