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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 kcal/mol. The calculated difference in the free energy of catalysis was 1.48 +/- 0.89 kcal/mol. These calculated values...

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PMID: 1904871

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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