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Fersht

Showing results (111-120 of 593) with videos related to

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FEBS Letters|November 4, 1991
Cooperativity in ATP hydrolysis by GroEL is increased by GroEST E Gray, A R Fersht
Biochemistry|December 29, 1987
Investigation of transition-state stabilization by residues histidine-45 and threonine-40 in the tyrosyl-tRNA synthetaseR J Leatherbarrow, A R Fersht
Biochemistry|April 22, 1986
Internal thermodynamics of position 51 mutants and natural variants of tyrosyl-tRNA synthetaseC K Ho, A R Fersht
Proceedings of the National Academy of Sciences of the United States of America|April 30, 1996
Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cageF J Corrales, A R Fersht
Nature Structural Biology|January 14, 1999
Upper limit of the time scale for diffusion and chain collapse in chymotrypsin inhibitor 2A G Ladurner, A R Fersht
Biochemistry|October 29, 1991
Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of foldingS E Jackson, A R Fersht
Biochemistry|December 14, 1993
Involvement of threonine 234 in catalysis of tyrosyl adenylate formation by tyrosyl-tRNA synthetaseE A First, A R Fersht
Biochemistry|July 26, 1988
Tyrosyl-tRNA synthetase acts as an asymmetric dimer in charging tRNA. A rationale for half-of-the-sites activityW H Ward, A R Fersht
Biochemistry|February 22, 1994
Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76-A resolutionA M Buckle, A R Fersht
Journal of Molecular Biology|August 20, 1993
Refolding of barnase in the presence of GroET E Gray, A R Fersht
Pageof 60

Showing results (111-120 of 593) with videos related to

Sort By:
Pageof 60
FEBS Letters|November 4, 1991
Cooperativity in ATP hydrolysis by GroEL is increased by GroEST E Gray, A R Fersht
Biochemistry|December 29, 1987
Investigation of transition-state stabilization by residues histidine-45 and threonine-40 in the tyrosyl-tRNA synthetaseR J Leatherbarrow, A R Fersht
Biochemistry|April 22, 1986
Internal thermodynamics of position 51 mutants and natural variants of tyrosyl-tRNA synthetaseC K Ho, A R Fersht
Proceedings of the National Academy of Sciences of the United States of America|April 30, 1996
Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cageF J Corrales, A R Fersht
Nature Structural Biology|January 14, 1999
Upper limit of the time scale for diffusion and chain collapse in chymotrypsin inhibitor 2A G Ladurner, A R Fersht
Biochemistry|October 29, 1991
Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of foldingS E Jackson, A R Fersht
Biochemistry|December 14, 1993
Involvement of threonine 234 in catalysis of tyrosyl adenylate formation by tyrosyl-tRNA synthetaseE A First, A R Fersht
Biochemistry|July 26, 1988
Tyrosyl-tRNA synthetase acts as an asymmetric dimer in charging tRNA. A rationale for half-of-the-sites activityW H Ward, A R Fersht
Biochemistry|February 22, 1994
Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76-A resolutionA M Buckle, A R Fersht
Journal of Molecular Biology|August 20, 1993
Refolding of barnase in the presence of GroET E Gray, A R Fersht
Pageof 60