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Nature|April 23, 1987
Conversion of allosteric inhibition to activation in phosphofructokinase by protein engineeringF T Lau, A R FershtJournal of Molecular Biology|November 21, 1997
Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding ratesA G Ladurner, A R FershtJournal of Molecular Biology|August 5, 1984
Fidelity of DNA replication under conditions used for oligodeoxynucleotide-directed mutagenesisJ P Shi, A R FershtProceedings of the National Academy of Sciences of the United States of America|June 6, 1995
The folding of GroEL-bound barnase as a model for chaperonin-mediated protein foldingF J Corrales, A R FershtBiochemistry|April 18, 1995
Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cyclesE A First, A R FershtBiochemistry|November 22, 1994
Contribution of residues in the reactive site loop of chymotrypsin inhibitor 2 to protein stability and activityS E Jackson, A R FershtBiochemistry|May 25, 1993
Use of binding energy in catalysis: optimization of rate in a multistep reactionJ M Avis, A R FershtBiochemistry|August 22, 1989
Dissection of the effector-binding site and complementation studies of Escherichia coli phosphofructokinase using site-directed mutagenesisF T Lau, A R FershtBiochemistry|April 22, 1986
Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-tRNA synthetaseT N Wells, A R FershtFEBS Letters|November 4, 1991
Cooperativity in ATP hydrolysis by GroEL is increased by GroEST E Gray, A R FershtPageof 36