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
Intrachain potential energy of the α-helix and of a coiled coil strand
✍ Scribed by D. A. D. Tarry; E. Suzuki
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1969
- Tongue
- English
- Weight
- 369 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
A comparison has been made of the intrachain potential energy of an infinite straight a-helix of poly-L-alanine with that of the distorted form adopted in a coiled coil conformation. The energy terms included were the van der Waal's, electrostatic, hydrogen-bond, and the rotational potential terms. The results indicate that the potential energies of the structures investigated are almost the same, and so a transformation from one state to another may occur without significant changes in potential energy.
Particular care has been taken to ensure that the electrostatic and van der Waal's interaction terms are fully convergent. The values obtained for the a-helix were compared with those already published, and some significant differences were found.
📜 SIMILAR VOLUMES
## Abstract Monte‐Carlo calculations of geometric and thermodynamic characteristics of the α‐helix and the β‐structure of polypeptides have been carried out. To describe a hydrogen bond both the Lippincott–Schroeder and Morse potentials were used. The internal rotation angles φ and ψ in the α‐helix
## SYNOPSIS Circular dichroism (CD) experiments in the backbone (200-240 n m ) region are reported for four isolated, excised two-chain, coiled-coil segments whose chains comprise, respectively, residues 11-127,142-281,l-189, and 190-284 of the rabbit aa-tropomyosin ( T m ) sequence. The uv and CD
Two extant models of thermal folding/unfolding equilibria in two-chain, @-helical coiled coils are tested by comparison with experimental results on excised, isolated subsequences of rabbit @a-tropomyosin ( T m ) . These substances are designated ;Tm, where i a n d j are, respectively, the residue n