## 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
.alpha.-Helix to random-coil transition of two-chain, coiled coils: experiments on the thermal denaturation of doubly crosslinked dimeric .beta.-tropomyosin
โ Scribed by Emerson Holtzer, Marilyn; Askins, Kelly; Holtzer, Alfred
- Book ID
- 126801369
- Publisher
- American Chemical Society
- Year
- 1986
- Tongue
- English
- Weight
- 606 KB
- Volume
- 25
- Category
- Article
- ISSN
- 0006-2960
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๐ SIMILAR VOLUMES
A method is described for preparation of a species of 88 tropomyosin that is sulfhydryl-blocked at C36 and disulfide-cross-linked at C190. Five steps are involved: (1) Rabbit skeletal muscle tropomywin, comprising aa and a8 species, is oxidized with ferricyanide, &sulfide-cross-linking both species
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
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