Non-uniform triple helical structure in chick skin type I collagen on thermal denaturation: Raman spectroscopic study
| Autor: | J. C. Dobbs, T. W. Collette, G. Chandraksasan, V. Renugopalakrishnan, R.C. Lord, L.A. Carreira |
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| Rok vydání: | 1998 |
| Předmět: |
Thermal denaturation
Protein Denaturation Hot Temperature Skin type Chemistry Solid-state Spectrum Analysis Raman General Biochemistry Genetics and Molecular Biology Protein Structure Secondary Crystallography symbols.namesake symbols Peptide bond Animals Thermodynamics Denaturation (biochemistry) Collagen Raman spectroscopy Chickens Triple helix Polyproline helix Skin |
| Zdroj: | Zeitschrift fur Naturforschung. C, Journal of biosciences. 53(5-6) |
| ISSN: | 0939-5075 |
| Popis: | The individual chains in the triple helix of collagen occur in a conformation related to polyproline II because of the presence of large number of imino peptide bonds. However, these residues are not evenly distributed in the collagen molecule which also contains many non-imino residues. These non-imino regions of collagen may be expected to show preference for other than triple helical conformations. The appearance of several Raman bands in solution phase at 65 °C raises the possibility of non-uniform triple helical structure in collagen. Raman spectroscopic studies on collagen in the solid state and in solution at a temperature greater than its denaturation temperature, reported here suggest that denatured collagen may exhibit an ensemble of conformational states with yet unknown implications to the biochemical interactions of this important protein component of connective tissues. |
| Databáze: | OpenAIRE |
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