?-Helix to random-coil transitions of two-chain coiled coils: The use of physical models in treating thermal denaturation equilibria of isolated subsequences of ??-tropomyosin-Reference-Cited by-同舟云学术

?-Helix to random-coil transitions of two-chain coiled coils: The use of physical models in treating thermal denaturation equilibria of isolated subsequences of ??-tropomyosin

Published:1990 Issue:13-14 Volume:30 Page:1231-1241
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Holtzer Alfred,Holtzer Marilyn Emerson

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference43 articles.

1. & (1973) Conformation in Fibrous Proteins, Academic, New York, pp. 419-468.

2. Streptococcal M protein: alpha-helical coiled-coil structure and arrangement on the cell surface.

3. Tropomyosin-like seven residue periodicity in three immunologically distinct streptococal M proteins and its implications for the antiphagocytic property of the molecule.

4. α-Helical coiled coils and bundles: How to design an α-helical protein

5. The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins

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1. Intrahelical Interactions in an α-Helical Coiled Coil Determine the Structural Stability of Tropomyosin;Biochemistry;2020-05-29

2. Effect of chain length on coiled-coil stability: Decreasing stability with increasing chain length;Biopolymers;2004

3. CD and13C?-NMR studies of folding equilibria in a two-stranded coiled coil formed by residues 190-254 of ?-tropomyosin;Biopolymers;2001

4. The use of spectral decomposition via the convex constraint algorithm in interpreting the CD-observed unfolding transitions of C coils;Biopolymers;1995-09

5. Structural stability of short subsequences of the tropomyosin chain;Biopolymers;1995-01