Cold denaturation of a synthetic collagen mimetic

Cold denaturation of a synthetic collagen mimetic

The cold denaturation of a synthetic collagen peptidomimetic in EG /H sub(2)O solutions was documented. The triple helix of Ac-(Gly-Pro-Nleu) sub(9)-NH sub(2) was found to undergo cold denaturation based on parabolic-like melting curves as well as changes in CD spectra. The experimental data also su...

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Veröffentlicht in:BIOPOLYM 1998-04, Vol.45 (5), p.347-350
Hauptverfasser: Feng, Yangbo, Jefferson, Elizabeth Anne, Goodman, Murray
Format: Artikel
Sprache:eng
Schlagworte:
Biosynthesis
Circular Dichroism
Cold Temperature
Collagen - analogs & derivatives
Collagen - chemistry
Cooling
Dissociation
Melting
Optical variables measurement
Peptides - chemistry
Polypeptides
Protein Conformation
Protein Denaturation - physiology
Protein Folding
Protein Structure, Tertiary
Spectroscopy
Stability
Structure (composition)
Temperature
Thermodynamics
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Beschreibung
Zusammenfassung:The cold denaturation of a synthetic collagen peptidomimetic in EG /H sub(2)O solutions was documented. The triple helix of Ac-(Gly-Pro-Nleu) sub(9)-NH sub(2) was found to undergo cold denaturation based on parabolic-like melting curves as well as changes in CD spectra. The experimental data also suggest that different structures of Ac-(Gly-Pro-Nleu) sub(9)-NH sub(2) are obtained from cold and heat denaturation.
ISSN:0006-3525
1097-0282
DOI:10.1002/(SICI)1097-0282(19980415)45:5<347::AID-BIP2>3.0.CO;2-L