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Molekuliarnaia Biologiia|November 1, 1987

[Substrate specificity of tyrosine-phenol-lyase. Electron and steric control at the stage of aromatic moiety elimination]N G Faleev, S B Ruvinov, V I Bakhmutov, et al.

Molekuliarnaia Biologiia|January 1, 1988

[Interaction of tyrosine-phenol-lyase from Citrobacter intermedius with amino acids and their derivatives: factors determining the effectiveness of binding]N G Faleev, S B Ruvinov, T V Demidkina, et al.

Protein Science : a Publication of the Protein Society|July 13, 2000

Conformational stability changes of the amino terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate: sugar phosphotransferase system produced by substituting alanine or glutamate for the active-site histidine 189: implications for phosphorylation effectsA Ginsburg, R H Szczepanowski, S B Ruvinov, et al.

Molekuliarnaia Biologiia|May 1, 1991

[Factors, determining the effectiveness of tryptophanase interaction with amino acids]N G Faleev, S B Ruvinov, L N Zakomyrdina, et al.

European Journal of Biochemistry|November 1, 1988

Tyrosine phenol-lyase from Citrobacter intermedius. Factors controlling substrate specificityN G Faleev, S B Ruvinov, T V Demidkina, et al.

The Journal of Biological Chemistry|March 17, 1995

Ligand-mediated changes in the tryptophan synthase indole tunnel probed by nile red fluorescence with wild type, mutant, and chemically modified enzymesS B Ruvinov, X J Yang, K D Parris, et al.

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Showing results (11-20 of 16) with videos related to

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You have reached the last page of results.This site can display upto 16 results.

Molekuliarnaia Biologiia|November 1, 1987

[Substrate specificity of tyrosine-phenol-lyase. Electron and steric control at the stage of aromatic moiety elimination]N G Faleev, S B Ruvinov, V I Bakhmutov, et al.

Molekuliarnaia Biologiia|January 1, 1988

[Interaction of tyrosine-phenol-lyase from Citrobacter intermedius with amino acids and their derivatives: factors determining the effectiveness of binding]N G Faleev, S B Ruvinov, T V Demidkina, et al.

Protein Science : a Publication of the Protein Society|July 13, 2000

Conformational stability changes of the amino terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate: sugar phosphotransferase system produced by substituting alanine or glutamate for the active-site histidine 189: implications for phosphorylation effectsA Ginsburg, R H Szczepanowski, S B Ruvinov, et al.

Molekuliarnaia Biologiia|May 1, 1991

[Factors, determining the effectiveness of tryptophanase interaction with amino acids]N G Faleev, S B Ruvinov, L N Zakomyrdina, et al.

European Journal of Biochemistry|November 1, 1988

Tyrosine phenol-lyase from Citrobacter intermedius. Factors controlling substrate specificityN G Faleev, S B Ruvinov, T V Demidkina, et al.

The Journal of Biological Chemistry|March 17, 1995

Ligand-mediated changes in the tryptophan synthase indole tunnel probed by nile red fluorescence with wild type, mutant, and chemically modified enzymesS B Ruvinov, X J Yang, K D Parris, et al.

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