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Article

Free energy perturbation techniques applied to subtilisin BPN' stability.

Advances in experimental medicine and biology - 1 Jan 1996

Barnett B L, Turner C B

Abstract excerpt

The inability to predict the effect of specific mutations on protein stability has been an area of concern to researchers in the field of protein engineering. Small stabilization free energies (5 to 15 kcal/mol) distinguish the native and the denatured states of a protein, making the rational design of protein stability a difficult challenge. Free Energy Perturbation Technique (FEPT) appears to be a method that...

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PMID: 8796316
DOI: 10.1007/978-1-4613-0319-0_13

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Free energy perturbation techniques applied to subtilisin BPN' stability.PMID 8796316Read ↗

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Can the stability of protein mutants be predicted by free energy calculations?Semantic proximity Read ↗

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Crystal structure analysis of subtilisin BPN' mutants engineered for studying thermal stability.Semantic proximity Read ↗

Structural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'.Semantic proximity Read ↗

Stabilizing mutations and calcium-dependent stability of subtilisin.Semantic proximity Read ↗

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