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α-Helix-to-random-coil transition of two-chain, coiled coils. Theory and experiments for thermal denaturation of α-tropomyosin at acidic pH

✍ Scribed by Holtzer, Marilyn Emerson; Holtzer, Alfred; Skolnick, Jeffrey

Book ID
126160314
Publisher
American Chemical Society
Year
1983
Tongue
English
Weight
521 KB
Volume
16
Category
Article
ISSN
0024-9297

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α-Helix to random coil transitions of tw
α-Helix to random coil transitions of two-chain coiled coils: Experiments on the thermal denaturation of isolated segments of αα-tropomyosin
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## 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

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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

α-Helix to random-coil transitions of tw
α-Helix to random-coil transitions of two-chain coiled coils: The use of physical models in treating thermal denaturation equilibria of isolated subsequences of αα-tropomyosin
✍ Alfred Holtzer; Marilyn Emerson Holtzer 📂 Article 📅 1990 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 983 KB

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