Temperature-Dependent Helix−Coil Transition of an Alanine Based Peptide
✍ Scribed by Huang, Cheng-Yen; Klemke, Jason W.; Getahun, Zelleka; DeGrado, William F.; Gai, Feng
- Book ID
- 126187914
- Publisher
- American Chemical Society
- Year
- 2001
- Tongue
- English
- Weight
- 61 KB
- Volume
- 123
- Category
- Article
- ISSN
- 0002-7863
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📜 SIMILAR VOLUMES
Thermal unfolding curves have been measured for a series of short alanine-based peptides that contain repeating sequences and varying chain lengths. Standard helix-coil theory successfully fits the observed transition curves, even for these short peptides. The results provide values for u, the helix
## Abstract The changes in the partial molar volume (PMV) associated with the conformational transition of an alanine‐rich peptide AK16 from the α‐helix structure to various random coil structures are calculated by the three‐dimensional interaction site model (3D‐RISM) theory coupled with the Kirkw
Thermal denaturation of DNA's and the corresponding helix-coil transformation of artificial polyribonucleic and polydeoxyribonucleic acids have been studied extensively both theoretically1-l3 and e ~p e r i m e n t a l l y . l ~-~~ Much less work has been carried out on the properties of these polyn