The Role of Cis-Trans Isomerization of Peptide Bonds in the Coil Triple Helix Conversion of Collagen
Open Access
- 1 October 1978
- journal article
- Published by Wiley in JBIC Journal of Biological Inorganic Chemistry
- Vol. 90 (3), 605-613
- https://doi.org/10.1111/j.1432-1033.1978.tb12641.x
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Three Conformationally Distinct Domains in the Amino-Terminal Segment of Type III Procollagen and Its Rapid Triple Helix Coil TransitionEuropean Journal of Biochemistry, 1978
- Test of the extended two-state model for the kinetic intermediates observed in the folding transition of ribonuclease AJournal of Molecular Biology, 1978
- Cis‐Trans equilibrium and kinetic studies of acetyl‐L‐proline and glycyl‐L‐prolinePeptide Science, 1977
- Nmr studies of the molecular conformations in the linear oligopeptides H‐(L‐Ala)n‐L‐Pro‐OHPeptide Science, 1976
- Molecular dynamics and structure of the random coil and helical states of the collagen peptide, α1-CB2, as determined by 13C magnetic resonanceBiochemistry, 1975
- Analysis of the helix–coil transition in (Pro‐Pro‐Gly)n by the All‐or‐none modelPeptide Science, 1973
- Evidence for cis peptide bonds in copolypeptides of glycine and prolineBiochemistry, 1972
- Co-operative non-enzymatic base recognition III. Kinetics of the helix—coil transition of the oligoribouridylic · oligoriboadenylic acid system and of oligoriboadenylic acid alone at acidic pHJournal of Molecular Biology, 1971
- A cooperative transition between two helical conformations in a linear system: poly-L-proline I ⇌ II. II. Kinetic studiesPeptide Science, 1971
- The Configurational Changes of Poly-L-proline in SolutionJournal of the American Chemical Society, 1960