A scanning calorimetric study of unfolding equilibria in homodimeric chicken gizzard tropomyosins

Biophysical Journal

Volumn 70, Issue 5, 1996, Pages 2403-2407

  O'Brien, Ronan ^a   Sturtevant, Julian M ^a   Wrabl, James ^b   Holtzer, Marilyn Emerson ^b   Holtzer, Alfred ^b  

^a YALE UNIVERSITY   (United States)

^b WASHINGTON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

TROPOMYOSIN;

ARTICLE; AVIAN STOMACH; CHICKEN; DIFFERENTIAL SCANNING CALORIMETRY; NONHUMAN; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AVES; GALLUS GALLUS; ORYCTOLAGUS CUNICULUS;

EID: 0029913321     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79808-9     Document Type: Article

References (14)

1. Cohen, C., and D. L. D. Parry. 1990. α-Helical coiled coils and bundles: how to design an α-helical protein. Proteins. 7:1-15
2. Holtzer, A., M. E. Holtzer, and J. Skolnick. 1990. Does the unfolding transition of two-chain, coiled-coil proteins involve a continuum of intermediates? In Protein Folding. L. M. Gierasch and J. King, editors. AAAS Books, Washington, DC. 177-190.
3. Holtzer, M. E., K. Askins, and A. Holtzer. 1986. α-Helix to random-coil transitions of two-chain coiled coils: experiments on the thermal denaturation of doubly cross-linked ββ tropomyosin. Biochemistry. 25: 1688-1692.
4. Holtzer, M. E., A. Holtzer, and J. Skolnick. 1983. The α-helix-to-random-coil transition of two-chain, coiled coils. Theory and experiments for thermal denaturation of α-tropomyosin. Macromolecules. 16:173-180.
5. Isom, L. L., M. E. Holtzer, and A. Holtzer. 1984. The α-helix-to-random-coil transition of two-chain, coiled coils. Experiments on the thermal denaturation of α-tropomyosin and β-tropomyosin. Macromolecules. 17:2445-2447.
6. Lehrer, S. S. 1978. Effects of an interchain disulfide bond on tropomyosin structure: intrinsic fluorescence and circular dichroism studies. J. Mol. Biol. 118:209-226.
7. Lehrer, S. S., and W. F. Stafford, III. 1991. Preferential assembly of the tropomyosin heterodimer: equilibrium studies. Biochemistry. 30: 5682-5688.
8. McLachlan, A. D., and M. Stewart. 1975. Tropomyosin coiled-coil interactions: evidence for an unstaggered structure. J. Mol. Biol. 98: 293-304.
9. Privalov, P. L. 1980. Scanning microcalorimeters for studying macromolecules. Pure Appl. Chem. 52:479-497.
10. Privalov, P. L. 1982. Stability of proteins: proteins which do not present a single cooperative system. Adv. Protein Chem. 35:1-104.
11. Skolnick, J., and A. Holtzer. 1986. α-Helix-to-random-coil transitions of two-chain, coiled coils: a theoretical model for the "pretransition" in cysteme-190-cross-lmked tropomyosin. Biochemistry. 25:6192-6202.
12. Srurtevant, J. M. 1987. Biochemical applications of differential scanning calorimetry. Annu. Rev. Phys. Chem. 38:463-488.
13. Sturtevant, J. M., M, E. Holtzer, and A. Holtzer. 1991. A scanning calorimetric study of the thermally induced unfolding of various forms of tropomyosin. Biopolymers. 31:489-495.
14. Wrabl, J., M. E. Holtzer, and A. Holtzer. 1994. Thermal unfolding equilibria m homodimeric chicken gizzard tropomyosin coiled coils. Biopolymers. 34:1659-1667.