Article
Conferring thermostability to mesophilic proteins through optimized electrostatic surfaces.
Biophysical journal - 1 Nov 2003
Torrez Michael, Schultehenrich Michael, Livesay Dennis R
Abstract excerpt
Recently, there have been several experimental reports of proteins displaying appreciable stability gains through mutation of one or two amino acid residues. Here, we employ a simple theoretical model to quickly screen mutant structures for increased thermostability through optimization of the protein's electrostatic surface. Our results are able to reproduce the experimental observation that elimination of...
Topics
- Amino Acid Sequence
- Archaeal Proteins
- Bacterial Proteins
- Computer Simulation
- Enzyme Stability
- Heat-Shock Proteins
- Membrane Proteins
- Methyl-Accepting Chemotaxis Proteins
- Models, Molecular
- Molecular Sequence Data
- Motion
- Mutation
- Protein Conformation