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Journal of Molecular Biology|February 12, 1998
Folding of barnase in the presence of the molecular chaperone SecBG Stenberg, A R FershtJournal of Molecular Biology|April 5, 1992
Co-operative interactions during protein foldingA Horovitz, A R FershtBiochemistry|May 28, 1996
New approach to the study of transient protein conformations: the formation of a semiburied salt link in the folding pathway of barnaseM Oliveberg, A R FershtBiochemistry|February 27, 1996
Thermodynamics of transient conformations in the folding pathway of barnase: reorganization of the folding intermediate at low pHM Oliveberg, A R FershtNucleic Acids Research|July 10, 1981
Alternative pathways for editing non-cognate amino acids by aminoacyl-tRNA synthetasesH Jakubowski, A R FershtJournal of Molecular Biology|September 24, 1999
Identification of substrate binding site of GroEL minichaperone in solutionN Tanaka, A R FershtBiochemistry|May 18, 1993
Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineeringG Schreiber, A R FershtBiochemistry|April 27, 1993
Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturationJ Clarke, A R FershtJournal of Molecular Biology|April 28, 1995
Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cyclesG Schreiber, A R FershtPageof 36