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Biochemistry|May 23, 1995
Protein stability as a function of denaturant concentration: the thermal stability of barnase in the presence of ureaC M Johnson, A R FershtBiochemistry|May 23, 1995
Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnaseJ M Matthews, A R FershtFEBS Letters|May 16, 1994
Measurement of barnase refolding rate constants under denaturing conditionsJ M Sanz, A R FershtBiochemistry|December 14, 1993
Mutational and kinetic analysis of a mobile loop in tyrosyl-tRNA synthetaseE A First, A R FershtBiochemistry|December 21, 1993
Contribution of long-range electrostatic interactions to the stabilization of the catalytic transition state of the serine protease subtilisin BPN'S E Jackson, A R FershtProtein Engineering|February 1, 1991
Linear free energy relationships in enzyme binding interactions studied by protein engineeringA R Fersht, T N WellsBiochemistry|October 29, 1991
Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transitionS E Jackson, A R FershtNature|August 6, 1987
Rational modification of enzyme catalysis by engineering surface chargeA J Russell, A R FershtBiochemistry|July 9, 1991
Fluorescence spectrum of barnase: contributions of three tryptophan residues and a histidine-related pH dependenceR Loewenthal, J Sancho, A R FershtPageof 36