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Helix Folding of an Alanine-Based Peptide in Explicit Water

✍ Scribed by Wu, Xiongwu; Wang, Shaomeng


Book ID
126933508
Publisher
American Chemical Society
Year
2001
Tongue
English
Weight
355 KB
Volume
105
Category
Article
ISSN
0022-3654

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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

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✍ Beatrice M. P. Huyghues-Despointes; J. Martin Scholtz; Robert L. Baldwin πŸ“‚ Article πŸ“… 1993 πŸ› Cold Spring Harbor Laboratory Press 🌐 English βš– 827 KB

## Abstract A single aspartate residue has been placed at various positions in individual peptides for which the alanine‐based reference peptide is electrically neutral, and the helix contents of the peptides have been measured by circular dichroism. The dependence of peptide helix content on aspar