Competition for hydrogen-bond formation in the helix-coil transition and protein folding
✍ Scribed by Badasyan, A. V.; Tonoyan, Sh. A.; Mamasakhlisov, Y. Sh.; Giacometti, Achille; Benight, A. S.; Morozov, V. F.
- Book ID
- 121481731
- Publisher
- The American Physical Society
- Year
- 2011
- Tongue
- English
- Weight
- 348 KB
- Volume
- 83
- Category
- Article
- ISSN
- 1063-651X
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📜 SIMILAR VOLUMES
To determine when secondary structure forms as two chains coalesce to form an alpha-helical dimer, the folding rates of variants of the coiled coil region of GCN4 were compared. Residues at non-perturbing positions along the exterior length of the helices were substituted one at a time with alanine
## Abstract We prepared a set of about 2000 α‐helices from a relational database of high‐resolution three‐dimensional structures of globular proteins, and identified additional main chain __i__ ← __i__+3 hydrogen bonds at the ends of the helices (i.e., where the hydrogen bonding potential is not fu