Free energy perturbation calculations on binding and catalysis after mutating threonine 220 in subtilisin.

Article

Free energy perturbation calculations on binding and catalysis after mutating threonine 220 in subtilisin.

The Journal of biological chemistry - 25 Jun 1991

Mizushima N, Spellmeyer D, Hirono S, Pearlman D, Kollman P

Abstract excerpt

We present the results of free energy perturbation calculations on binding and catalysis of a tetrapeptide substrate, acetyl-Phe-Ala-Ala-Phe-NMe, by native subtilisin BPN' and a subtilisin BPN' mutant (Thr220----Ala220). The calculated difference in the free energy of binding was 0.70 +/- 0.72 kc...

Topics

Amino Acid Sequence
Amino Acids
Bacillus subtilis
Binding Sites
Catalysis
Molecular Sequence Data
Mutation
Protein Conformation
Substrate Specificity
Subtilisins
Thermodynamics

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