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.alpha.-Helix to random-coil transition of two-chain, coiled coils: experiments on the thermal denaturation of doubly crosslinked dimeric .beta.-tropomyosin

โœ 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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๐Ÿ“œ SIMILAR VOLUMES


ฮฑ-Helix to random coil transitions of tw
โœ Marilyn Emerson Holtzer; Alfred Holtzer ๐Ÿ“‚ Article ๐Ÿ“… 1990 ๐Ÿ› Wiley (John Wiley & Sons) ๐ŸŒ English โš– 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

ฮฑ-Helix-to-random-coil transitions of tw
โœ William Clay Bracken; John Carey; Marilyn Emerson Holtzer; Alfred Holtzer ๐Ÿ“‚ Article ๐Ÿ“… 1988 ๐Ÿ› Wiley (John Wiley & Sons) ๐ŸŒ English โš– 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

ฮฑ-Helix to random-coil transitions of tw
โœ Alfred Holtzer; Marilyn Emerson Holtzer ๐Ÿ“‚ Article ๐Ÿ“… 1990 ๐Ÿ› Wiley (John Wiley & Sons) ๐ŸŒ English โš– 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

Application of the augmented theory of ฮฑ
โœ Alfred Holtzer; Jeffrey Skolnick ๐Ÿ“‚ Article ๐Ÿ“… 1988 ๐Ÿ› Wiley (John Wiley & Sons) ๐ŸŒ English โš– 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