Article
Stability and solvation of Thr/Ser to Ala and Gly mutations at the N-cap of alpha-helices.
FEBS letters - 27 Jun 1994
Chen Y W, Fersht A R
Abstract excerpt
The solvation of polar groups at the N-terminal end of alpha-helices was studied by comparing the crystal structures of T4 lysozyme, barley chymotrypsin inhibitor 2 (CI2), barnase and their respective N-cap mutants. Whether or not the N3 residue is solvated on mutating the N-cap Thr/Ser to Ala or...
Topics
- Bacterial Proteins
- Bacteriophage T4
- Computer Simulation
- Crystallization
- Enzyme Stability
- Hydrogen Bonding
- Models, Molecular
- Molecular Structure
- Muramidase
- Mutation
- Peptides
- Plant Proteins
- Protein Conformation