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C R Matthews

Showing results (21-30 of 82) with videos related to

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Biochemistry|December 8, 1998
Mechanism of folding of the dimeric core domain of Escherichia coli trp repressor: a nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediateL M Gloss, C R Matthews
Biochemistry|August 6, 1999
Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain proteinJ A Zitzewitz, C R Matthews
Biochemistry|February 27, 1990
Role of diffusion in the folding of the alpha subunit of tryptophan synthase from Escherichia coliB A Chrunyk, C R Matthews
Biochemistry|May 25, 1993
Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate bindingC J Mann, C R Matthews
Biochemistry|May 13, 1997
Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressorL M Gloss, C R Matthews
Biochemistry|October 7, 1975
Nuclear magnetic resonance studies of residual structure in thermally unfolded ribonuclease AC R Matthews, D G Westmoreland
Biochimica Et Biophysica Acta|June 17, 1987
Proline isomerization and the slow folding reactions of the alpha subunit of tryptophan synthase from Escherichia coliM R Hurle, C R Matthews
Proceedings of the National Academy of Sciences of the United States of America|March 1, 1973
Nuclear magnetic resonance study of the thermal denaturation of ribonuclease A: implications for multistate behavior at low pHD G Westmoreland, C R Matthews
Protein Science : a Publication of the Protein Society|February 1, 1995
Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMRB E Jones, C R Matthews
Biochemistry|August 22, 1995
Detection of a stable intermediate in the thermal unfolding of a cysteine-free form of dihydrofolate reductase from Escherichia coliJ Luo, M Iwakura, C R Matthews
Pageof 9

Showing results (21-30 of 82) with videos related to

Sort By:
Pageof 9
Biochemistry|December 8, 1998
Mechanism of folding of the dimeric core domain of Escherichia coli trp repressor: a nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediateL M Gloss, C R Matthews
Biochemistry|August 6, 1999
Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain proteinJ A Zitzewitz, C R Matthews
Biochemistry|February 27, 1990
Role of diffusion in the folding of the alpha subunit of tryptophan synthase from Escherichia coliB A Chrunyk, C R Matthews
Biochemistry|May 25, 1993
Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate bindingC J Mann, C R Matthews
Biochemistry|May 13, 1997
Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressorL M Gloss, C R Matthews
Biochemistry|October 7, 1975
Nuclear magnetic resonance studies of residual structure in thermally unfolded ribonuclease AC R Matthews, D G Westmoreland
Biochimica Et Biophysica Acta|June 17, 1987
Proline isomerization and the slow folding reactions of the alpha subunit of tryptophan synthase from Escherichia coliM R Hurle, C R Matthews
Proceedings of the National Academy of Sciences of the United States of America|March 1, 1973
Nuclear magnetic resonance study of the thermal denaturation of ribonuclease A: implications for multistate behavior at low pHD G Westmoreland, C R Matthews
Protein Science : a Publication of the Protein Society|February 1, 1995
Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMRB E Jones, C R Matthews
Biochemistry|August 22, 1995
Detection of a stable intermediate in the thermal unfolding of a cysteine-free form of dihydrofolate reductase from Escherichia coliJ Luo, M Iwakura, C R Matthews
Pageof 9