Structural characterization of the transition state for folding of muscle acylphosphatase.

doi:10.1006/jmbi.1998.2010

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Article

Structural characterization of the transition state for folding of muscle acylphosphatase.

Journal of molecular biology - 6 Nov 1998

Chiti F, Taddei N, van Nuland N A, Magherini F, Stefani M, Ramponi G, Dobson C M

Abstract excerpt

The transition state for folding of a small protein, muscle acylphosphatase, has been studied by measuring the rates of folding and unfolding under a variety of solvent conditions. A strong dependence of the folding rate on the concentration of urea suggests the occurrence in the transition state...

Topics

Acid Anhydride Hydrolases
Alcohols
Circular Dichroism
Cysteine
Fluorescence
Humans
Kinetics
Muscles
Mutation
Phosphates
Protein Folding
Temperature
Thermodynamics
Trifluoroethanol
Urea
Acylphosphatase

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