Article
Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles.
Biochemistry - 9 Oct 1990
Serrano L, Horovitz A, Avron B, Bycroft M, Fersht A R
Abstract excerpt
Coulombic interactions between charges on the surface of proteins contribute to stability. It is difficult, however, to estimate their importance by protein engineering methods because mutation of one residue in an ion pair alters the energetics of many interactions in addition to the coulombic e...
Topics
- Amino Acid Sequence
- Bacillus
- Bacterial Proteins
- Drug Stability
- Electrochemistry
- Endoribonucleases
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Protein Engineering
- Proteins
- Ribonucleases
- Surface Properties
- Thermodynamics
