The free energies for mutating S27 and W79 to alanine in streptavidin and its biotin complex: the relative size of polar and nonpolar free energies on biotin binding.
We have carried out calculations on the relative free energy of binding of biotin and its S27A and W79A mutants to streptavidin. Consistent with earlier suggestions by Miyamoto and Kollman from free energy component analysis and recent experiments by Stayton and coworkers, the reduction in binding strength by the W79A mutant is significantly larger than that of the S27A mutant. Proteins 1999;36:471-473.
Dixon
R W
RW
Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94143, USA.
Kollman
P
P
D000409:Alanine / Q000235:genetics; D019943:Amino Acid Substitution; D001710:Biotin / Q000378:metabolism*; D003198:Computer Simulation; D009154:Mutation; D011485:Protein Binding; D012694:Serine / Q000235:genetics; D055672:Static Electricity; D019809:Streptavidin / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013816:Thermodynamics; D014364:Tryptophan / Q000235:genetics
D012694:Serine; D001710:Biotin; D014364:Tryptophan; D019809:Streptavidin; D000409:Alanine