ArticleProtein science : a publication of the Protein Society2000
The design of a hyperstable mutant of the Abp1p SH3 domain by sequence alignment analysis.
Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 59 citations in OpenAlex.
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- Improved thermostability of creatinase from Alcaligenes Faecalis through non-biased phylogenetic consensus-guided mutagenesis.Microbial cell factories · 2020Article
- Analysis of Amylin Consensus Sequences Suggests That Human Amylin Is Not Optimized to Minimize Amyloid Formation and Provides Clues to Factors That Modulate Amyloidogenicity.ACS chemical biology · 2020Article
- Consensus sequence design as a general strategy to create hyperstable, biologically active proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- A multi-column plate adapter provides an economical and versatile high-throughput protein purification system.Protein expression and purification · 2018Article
- Comprehensive analysis of NMR data using advanced line shape fitting.Journal of biomolecular NMR · 2017Article
- Characterization of Reconstructed Ancestral Proteins Suggests a Change in Temperature of the Ancient Biosphere.Life (Basel, Switzerland) · 2017Review
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- Protein evolution analysis of S-hydroxynitrile lyase by complete sequence design utilizing the INTMSAlign software.Scientific reports · 2015Article
- PINT: a software for integration of peak volumes and extraction of relaxation rates.Journal of biomolecular NMR · 2013Article
- Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R(1ρ): an application to αB-crystallin.Journal of biomolecular NMR · 2012Article
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- Consensus protein design without phylogenetic bias.Journal of molecular biology · 2010Article
- Measuring 13Cbeta chemical shifts of invisible excited states in proteins by relaxation dispersion NMR spectroscopy.Journal of biomolecular NMR · 2009Article
- Isotope labeling methods for studies of excited protein states by relaxation dispersion NMR spectroscopy.Nature protocols · 2009Article
- Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively (13)C labeled samples.Journal of biomolecular NMR · 2008Article
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- Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain.Protein science : a publication of the Protein Society · 2006Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
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. Three of the eight mutants constructed in this way displayed increases in Tm ranging from 8 to 15 degrees C with concomitant increases in deltaGu of up to 1.4 kcal/mol. The effects of these substitutions on folding thermodynamics and kinetics were entirely additive, and a mutant containing all three was dramatically stabilized with a Tm greater than 90 degrees C and a deltaGu more than double that of the wild-type domain. The folding rate of this hyperstable mutant was 10-fold faster than wild-type, while its unfolding rate was fivefold slower. All of the stabilized mutants were still able to bind a target peptide with wild-type affinity. We have analyzed the stabilizing amino acid substitutions isolated in this study and several other similar sequence alignment based studies. In approximately 25% of cases, increased stability can be explained by enhanced propensity of the substituted residue for the local backbone conformation at the mutagenized site.
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