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

@article{Rath2000TheDO,
  title={The design of a hyperstable mutant of the Abp1p SH3 domain by sequence alignment analysis.},
  author={Arianna Rath and Alan R. Davidson},
  journal={Protein science : a publication of the Protein Society},
  year={2000},
  volume={9 12},
  pages={2457-69}
}
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 subsequently replaced by the residue seen most frequently at that position in the alignment… CONTINUE READING
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