Amino Acid Substitutions: Effects on Protein Stability
Zhiping Weng, Boston University, Boston, Massachusetts, USA
Charles DeLisi, Boston University, Boston, Massachusetts, USA
Published online: April 2001
The ability of a protein to function in its biochemical role(s) is determined by its geometry, which in turn is determined
by the amino acid sequence and the environment. Amino acid mutations affect the thermodynamics of folding and their effects
can be investigated experimentally by such techniques as site‐specific mutation, random point mutations and shuffling.
Keywords: protein stability; folding free energy; solvation; electrostatic interactions; site‐specific mutagenesis; random mutations
Baase WA and
A test of the „jigsaw puzzle” model for protein folding by multiple methionine substitutions within the core of T4 lysozyme.
Proceedings of the National Academy of Sciences of the USA
Protein folding from a combinatorial perspective.
Folding and Design
Rosenfeld R and
Effect of conformational flexibility and solvation on receptor ligand binding free energies.
Vajda S and
Rigid body docking with semi empirical free energy functions.
Branden C and
Introduction to Protein Structure.
New York: Garland Publishing.