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Theory of α-helix-to-random-coil transition of two-chain, coiled coils. Application of the augmented theory to thermal denaturation of ββ tropomyosin

✍ Scribed by Holtzer, Alfred; Skolnick, Jeffrey


Book ID
126935067
Publisher
American Chemical Society
Year
1986
Tongue
English
Weight
279 KB
Volume
19
Category
Article
ISSN
0024-9297

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📜 SIMILAR VOLUMES


α-Helix-to-random-coil transitions of tw
✍ William Clay Bracken; John Carey; Marilyn Emerson Holtzer; Alfred Holtzer 📂 Article 📅 1988 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 996 KB

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

Application of the augmented theory of α
✍ Alfred Holtzer; Jeffrey Skolnick 📂 Article 📅 1988 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 644 KB

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

α-Helix to random coil transitions of tw
✍ Marilyn Emerson Holtzer; Alfred Holtzer 📂 Article 📅 1990 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 817 KB

## 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