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Article

The design of a hyperstable mutant of the Abp1p SH3 domain by sequence alignment analysis.

Protein science : a publication of the Protein Society - 1 Dec 2000

Rath A, Davidson A R

Abstract excerpt

We have characterized the thermodynamic stability of the SH3 domain from the Saccharomyces cerevisiae Abp1p protein and found it to be relatively low compared to most other SH3 domains, with a Tm of 60 degrees C and a deltaGu of 3.08 kcal/mol. Analysis of a large alignment of SH3 domains led to the identification of atypical residues at eight positions in the wild-type Abp1p SH3 domain sequence that were...

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Identifiers

PMID: 11206067
DOI: 10.1110/ps.9.12.2457
PMCID: PMC2144507

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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