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Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition

Biochemistry

Mar 1, 1994

Ana Rosa VigueraLuis A Serrano

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Abstract

The folding and unfolding reactions of the SH3 domain of spectrin can be described by a two-state model. This domain is a beta-sheet barrel containing 62 amino acids. Equilibrium unfolding by urea, guanidine hydrochloride, and heat is completely reversible at pH values below 4.0. At hig...read more

Mentioned in this Paper

Thermodynamics
Spectrin Location
Guanidine Hydrochloride
Fluorescence Spectroscopy
Effects of Heat
Denaturation
Circular Dichroism, Vibrational
Protein Folding, Globular
Circular Dichroism
Urea
Paper Details
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Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition

Biochemistry

Mar 1, 1994

Ana Rosa VigueraLuis A Serrano

PMID: 7509635

DOI: 10.1021/bi00174a022

Abstract

The folding and unfolding reactions of the SH3 domain of spectrin can be described by a two-state model. This domain is a beta-sheet barrel containing 62 amino acids. Equilibrium unfolding by urea, guanidine hydrochloride, and heat is completely reversible at pH values below 4.0. At hig...read more

Mentioned in this Paper

Thermodynamics
Spectrin Location
Guanidine Hydrochloride
Fluorescence Spectroscopy
Effects of Heat
Paper Details
References
  • References
  • Citations174
  • References currently unavailable

    We're still populating references for this paper, please check back later.
  • References
  • Citations174
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