Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability.

@article{Serrano1993StepwiseMO,
  title={Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability.},
  author={L. Durb{\'a}n Serrano and Anthony G Day and A. R. Fersht},
  journal={Journal of molecular biology},
  year={1993},
  volume={233 2},
  pages={
          305-12
        }
}
We have chosen two members of the microbial RNase family, barnase and binase, which have 85% identity (17 substitutions and 1 deletion) and almost identical three-dimensional structure, to study the evolution of protein stability. The 17 residues that differ are scattered throughout the molecule. Each of the 17 differing residues has been mutated independently and the effect on protein stability analysed. Each point mutation has an effect on protein stability that ranges from +1.1 to -1.1 kcal… CONTINUE READING
Highly Cited
This paper has 99 citations. REVIEW CITATIONS

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 58 extracted citations

Contingency and entrenchment in protein evolution under purifying selection.

Proceedings of the National Academy of Sciences of the United States of America • 2015
View 6 Excerpts
Highly Influenced

Extreme functional sensitivity to conservative amino acid changes on enzyme exteriors.

Journal of molecular biology • 2000
View 4 Excerpts
Highly Influenced

100 Citations

0510'96'01'07'13'19
Citations per Year
Semantic Scholar estimates that this publication has 100 citations based on the available data.

See our FAQ for additional information.