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
Osmolyte effects on helix formation in peptides and the stability of coiled-coils
β Scribed by Scott A. Celinski; J. Martin Scholtz
- Book ID
- 119982927
- Publisher
- Cold Spring Harbor Laboratory Press
- Year
- 2002
- Tongue
- English
- Weight
- 74 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0961-8368
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π SIMILAR VOLUMES
A simple way to incorporate the solvent-peptide interaction in any available theory of the helix-coil transition is developed. The competition between the intramolecular hydrogen bonding and the solvent-polymer hydrogen bonding is considered in multicomponent solvents where some of the components ha
## Abstract The effect of magnesium ions on the parameters of the DNA helixβcoil transition has been studied for the concentration range 10^β6^β10^β1^__M__ at the ionic strengths of 10^β3^__M__ Na^+^. Special attention has been given to the region of low ion concentrations and to the effect of poly
The statistical mechanical theory for the helix-to-random-coil transition in two-chain coiled coils is applied to extant data for two synthetic coiled-coil polypeptides. These peptides have the primary structure K(LEALEGK),, in which n = 4,5. This repeating heptet sequence mimics the pattern of hydr