Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

Fersht

Showing results (141-150 of 593) with videos related to

Pageof 60
Sort By:
Folding & Design|January 1, 1996
Kinetic significance of GroEL14.(GroES7)2 complexes in molecular chaperone activityF J Corrales, A R Fersht
Biochemistry|June 12, 1998
Folding of circular and permuted chymotrypsin inhibitor 2: retention of the folding nucleusD E Otzen, A R Fersht
The EMBO Journal|June 10, 1998
Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domainM G Mateu, A R Fersht
Biochemistry|January 27, 1976
Subunit interactions in the methionyl-tRNA synthetase of Bacillus stearothermophilusR S Mulvey, A R Fersht
Biochemistry|November 23, 1982
Direct observation of complexes formed between recA protein and a fluorescent single-stranded deoxyribonucleic acid derivativeM S Silver, A R Fersht
Biochemistry|May 28, 1991
Correlations between kinetic and X-ray analyses of engineered enzymes: crystal structures of mutants Cys----Gly-35 and Tyr----Phe-34 of tyrosyl-tRNA synthetaseM D Fothergill, A R Fersht
Biochemistry|December 26, 1978
Mechanism of aminoacylation of transfer RNA. A pre-steady-state analysis of the reaction pathway catalyzed by the methionyl-tRNA synthetase of Bacillus stearothermophilusR S Mulvey, A R Fersht
Folding & Design|January 1, 1996
An NMR study on the beta-hairpin region of barnaseJ L Neira, A R Fersht
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 Fersht
Biochemistry|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 Fersht
Pageof 60

Showing results (141-150 of 593) with videos related to

Sort By:
Pageof 60
Folding & Design|January 1, 1996
Kinetic significance of GroEL14.(GroES7)2 complexes in molecular chaperone activityF J Corrales, A R Fersht
Biochemistry|June 12, 1998
Folding of circular and permuted chymotrypsin inhibitor 2: retention of the folding nucleusD E Otzen, A R Fersht
The EMBO Journal|June 10, 1998
Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domainM G Mateu, A R Fersht
Biochemistry|January 27, 1976
Subunit interactions in the methionyl-tRNA synthetase of Bacillus stearothermophilusR S Mulvey, A R Fersht
Biochemistry|November 23, 1982
Direct observation of complexes formed between recA protein and a fluorescent single-stranded deoxyribonucleic acid derivativeM S Silver, A R Fersht
Biochemistry|May 28, 1991
Correlations between kinetic and X-ray analyses of engineered enzymes: crystal structures of mutants Cys----Gly-35 and Tyr----Phe-34 of tyrosyl-tRNA synthetaseM D Fothergill, A R Fersht
Biochemistry|December 26, 1978
Mechanism of aminoacylation of transfer RNA. A pre-steady-state analysis of the reaction pathway catalyzed by the methionyl-tRNA synthetase of Bacillus stearothermophilusR S Mulvey, A R Fersht
Folding & Design|January 1, 1996
An NMR study on the beta-hairpin region of barnaseJ L Neira, A R Fersht
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 Fersht
Biochemistry|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 Fersht
Pageof 60