Thermodynamics of Formation of the Triple Helix from Free Chains and from Template-Constrained Chains of Collagen-like Monodisperse Poly(Gly-Pro-Hyp) Structures-Reference-Cited by-同舟云学术

Thermodynamics of Formation of the Triple Helix from Free Chains and from Template-Constrained Chains of Collagen-like Monodisperse Poly(Gly-Pro-Hyp) Structures

Published:1999-11-05 Issue:49 Volume:103 Page:10561-10566
ISSN:1089-5639
Container-title:The Journal of Physical Chemistry A
language:en
Short-container-title:J. Phys. Chem. A

Author:

Locardi Elsa¹,Kwak Juliann¹,Scheraga Harold A.¹,Goodman Murray¹

Affiliation:

1. Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, California 92093-0343, and Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp9925435

Reference14 articles.

1. Helix [UNK] Coil Transitions in Dilute Aqueous Collagen Solutions1

2. Collagen structure in solution. I. Kinetics of helix regeneration in single-chain gelatins

3. Analysis of the helix-coil transition in (Pro-Pro-Gly)n by the All-or-none model

4. Statistical thermodynamics of triple-helix unzippering for the collagen model (Gly-Pro-Pro)n and implications for natural collagen

5. Recursion relation generation of probability profiles for specific-sequence macromolecules with long-range correlations

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