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C R Matthews

Showing results (41-50 of 82) with videos related to

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Biochemistry|February 15, 2001
Mapping the energy surface for the folding reaction of the coiled-coil peptide GCN4-p1B Ibarra-Molero, G I Makhatadze, C R Matthews
Biochemistry|September 23, 1986
Folding of dihydrofolate reductase from Escherichia coliN A Touchette, K M Perry, C R Matthews
Biochemistry|February 14, 1995
Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopyB E Jones, J M Beechem, C R Matthews
Biochimica Et Biophysica Acta|August 21, 1980
The pentaammineruthenium(III)-histidine complex in ribonuclease A as an optical probe of conformational changeC R Matthews, P M Erickson, C L Froebe
Biochemistry|December 21, 1993
Urea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentrationG Saab-Rincón, C L Froebe, C R Matthews
Protein Science : a Publication of the Protein Society|September 23, 1997
Probing minimal independent folding units in dihydrofolate reductase by molecular dissectionC V Gegg, K E Bowers, C R Matthews
Protein Science : a Publication of the Protein Society|November 1, 1993
Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutantsC A Royer, C J Mann, C R Matthews
Journal of Molecular Biology|October 3, 2001
Rough energy landscapes in protein folding: dimeric E. coli Trp repressor folds through three parallel channelsL M Gloss, B R Simler, C R Matthews
Biochemistry|February 13, 1996
Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthaseG Saab-Rincón, P J Gualfetti, C R Matthews
Biochemistry|October 21, 1986
Synergism in folding of a double mutant of the alpha subunit of tryptophan synthaseM R Hurle, N B Tweedy, C R Matthews
Pageof 9

Showing results (41-50 of 82) with videos related to

Sort By:
Pageof 9
Biochemistry|February 15, 2001
Mapping the energy surface for the folding reaction of the coiled-coil peptide GCN4-p1B Ibarra-Molero, G I Makhatadze, C R Matthews
Biochemistry|September 23, 1986
Folding of dihydrofolate reductase from Escherichia coliN A Touchette, K M Perry, C R Matthews
Biochemistry|February 14, 1995
Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopyB E Jones, J M Beechem, C R Matthews
Biochimica Et Biophysica Acta|August 21, 1980
The pentaammineruthenium(III)-histidine complex in ribonuclease A as an optical probe of conformational changeC R Matthews, P M Erickson, C L Froebe
Biochemistry|December 21, 1993
Urea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentrationG Saab-Rincón, C L Froebe, C R Matthews
Protein Science : a Publication of the Protein Society|September 23, 1997
Probing minimal independent folding units in dihydrofolate reductase by molecular dissectionC V Gegg, K E Bowers, C R Matthews
Protein Science : a Publication of the Protein Society|November 1, 1993
Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutantsC A Royer, C J Mann, C R Matthews
Journal of Molecular Biology|October 3, 2001
Rough energy landscapes in protein folding: dimeric E. coli Trp repressor folds through three parallel channelsL M Gloss, B R Simler, C R Matthews
Biochemistry|February 13, 1996
Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthaseG Saab-Rincón, P J Gualfetti, C R Matthews
Biochemistry|October 21, 1986
Synergism in folding of a double mutant of the alpha subunit of tryptophan synthaseM R Hurle, N B Tweedy, C R Matthews
Pageof 9