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C R Matthews

Showing results (71-80 of 82) with videos related to

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Biochemistry|April 1, 1980
Effect of single amino acid substitutions on the thermal stability of the alpha subunit of tryptophan synthaseC R Matthews, M M Crisanti, G L Gepner, et al.
Biochemistry|January 26, 1988
Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybridsT M Stackhouse, J J Onuffer, C R Matthews, et al.
Journal of Molecular Biology|February 25, 2000
Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil systemJ A Zitzewitz, B Ibarra-Molero, D R Fishel, et al.
Protein Science : a Publication of the Protein Society|July 1, 1999
Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel proteinJ A Zitzewitz, P J Gualfetti, I A Perkons, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 18, 1997
Native-like structure of a protein-folding intermediate bound to the chaperonin GroELM S Goldberg, J Zhang, S Sondek, et al.
Methods in Enzymology|January 1, 1991
Mutational analysis of protein folding mechanismsP A Jennings, S M Saalau-Bethell, B E Finn, et al.
Proteins|January 1, 1987
Prediction of the tertiary structure of the alpha-subunit of tryptophan synthaseM R Hurle, C R Matthews, F E Cohen, et al.
Biochemistry|May 20, 1986
Effects of the phenylalanine-22----leucine, glutamic acid-49----methionine, glycine-234----aspartic acid, and glycine-234----lysine mutations on the folding and stability of the alpha subunit of tryptophan synthase from Escherichia coliA M Beasty, M R Hurle, J T Manz, et al.
Biochemistry|October 21, 1999
Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel proteinP J Gualfetti, M Iwakura, J C Lee, et al.
Journal of Biomolecular NMR|May 1, 1994
1H, 15N and 13C resonance assignments, secondary structure, and the conformation of substrate in the binary folate complex of Escherichia coli dihydrofolate reductaseC J Falzone, J Cavanagh, M Cowart, et al.
Pageof 9

Showing results (71-80 of 82) with videos related to

Sort By:
Pageof 9
Biochemistry|April 1, 1980
Effect of single amino acid substitutions on the thermal stability of the alpha subunit of tryptophan synthaseC R Matthews, M M Crisanti, G L Gepner, et al.
Biochemistry|January 26, 1988
Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybridsT M Stackhouse, J J Onuffer, C R Matthews, et al.
Journal of Molecular Biology|February 25, 2000
Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil systemJ A Zitzewitz, B Ibarra-Molero, D R Fishel, et al.
Protein Science : a Publication of the Protein Society|July 1, 1999
Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel proteinJ A Zitzewitz, P J Gualfetti, I A Perkons, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 18, 1997
Native-like structure of a protein-folding intermediate bound to the chaperonin GroELM S Goldberg, J Zhang, S Sondek, et al.
Methods in Enzymology|January 1, 1991
Mutational analysis of protein folding mechanismsP A Jennings, S M Saalau-Bethell, B E Finn, et al.
Proteins|January 1, 1987
Prediction of the tertiary structure of the alpha-subunit of tryptophan synthaseM R Hurle, C R Matthews, F E Cohen, et al.
Biochemistry|May 20, 1986
Effects of the phenylalanine-22----leucine, glutamic acid-49----methionine, glycine-234----aspartic acid, and glycine-234----lysine mutations on the folding and stability of the alpha subunit of tryptophan synthase from Escherichia coliA M Beasty, M R Hurle, J T Manz, et al.
Biochemistry|October 21, 1999
Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel proteinP J Gualfetti, M Iwakura, J C Lee, et al.
Journal of Biomolecular NMR|May 1, 1994
1H, 15N and 13C resonance assignments, secondary structure, and the conformation of substrate in the binary folate complex of Escherichia coli dihydrofolate reductaseC J Falzone, J Cavanagh, M Cowart, et al.
Pageof 9