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Kinetics of folding of αα-tropomyosin subsequences

✍ Scribed by Jianming Mo; Marilyn Emerson Holtzer; Alfred Holtzer

Publisher
Wiley (John Wiley & Sons)
Year
1992
Tongue
English
Weight
533 KB
Volume
32
Category
Article
ISSN
0006-3525

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Kinetics of folding and unfolding of αα-
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## Abstract Stopped flow CD (SFCD) kinetic studies of self–assembly of coiled coils of rabbit αα–tropomyosin and of nonpolymerizable αα–tropomyosin (NPTm) are reported. The protein was denatured in 6__M__ urea buffer, then renatured by 10‐fold dilution into benign saline buffer. Folding was monitor

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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
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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

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✍ Marilyn Emerson Holtzer; Dan L. Crimmins; Alfred Holtzer 📂 Article 📅 1995 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 1018 KB

## Abstract The native tropomyosin molecule is a parallel, registered, α‐helical coiled coil made from two 284‐residiic chains. Long excised subsequences (≥ 95 residues) form the same structure with comparable thermal stability. Here, we investigate local stability using shorter subsequences (20‐50

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## SYNOPSIS Measurements are presented on the time course of chain exchange among two-chain ahelical coiled coils of rabbit tropomyosin. All experiments are in a regime (temperature, protein concentration) in which coiled-coil dimers are the predominant species. Self-exchange in rue-tropomyosin wa