Synthesis and physical properties of (hydroxyproline-proline-glycine)10: Hydroxyproline in the X-position decreases the melting temperature of the collagen triple helix
- 1 November 1982
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 219 (1) , 198-203
- https://doi.org/10.1016/0003-9861(82)90149-7
Abstract
No abstract availableThis publication has 26 references indexed in Scilit:
- The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagenPublished by Elsevier ,2004
- Chain conformation in the collagen moleculeJournal of Molecular Biology, 1979
- Stability and mobility of the collagen structureJournal of Molecular Biology, 1979
- Molecular dynamics and structure of the random coil and helical states of the collagen peptide, α1-CB2, as determined by 13C magnetic resonanceBiochemistry, 1975
- Influence of proline hydroxylation upon the thermal stability of collagen fragment α1CB2Journal of Molecular Biology, 1973
- Hydroxyproline stabilizes the triple helix of chick tendon collagenBiochemical and Biophysical Research Communications, 1973
- Polymers of tripeptides as collagen models: VIII. X-ray studies of four polyhexapeptidesJournal of Molecular Biology, 1969
- Low temperature circular dichroism of poly (glycyl-l-prolyl-l-alanine)Journal of Molecular Biology, 1969
- Analysis of the Optical Rotatory Dispersion of Polypeptides and Proteins. IV. A Digital Computer Analysis for the Region 190-600 mμ1,2Journal of the American Chemical Society, 1966
- Polymers of tripeptides as collagen modelsJournal of Molecular Biology, 1966