Literature DB >> 4878703

Fluorescence studies of substrate and subunit interactions of the beta-2 protein of Escherichia coli tryptophan synthetase.

M E Goldberg, S York, L Stryer.   

Abstract

Entities:  

Mesh:

Substances:

Year:  1968        PMID: 4878703     DOI: 10.1021/bi00850a045

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


× No keyword cloud information.
  5 in total

Review 1.  Allosteric regulation of substrate channeling and catalysis in the tryptophan synthase bienzyme complex.

Authors:  Michael F Dunn
Journal:  Arch Biochem Biophys       Date:  2012-02-02       Impact factor: 4.013

2.  Preparation and characterization of a modified form of beta2 subunit of Escherichia coli tryptophan synthetase suitable for investigating protein folding.

Authors:  A Högberg-Raibaud; M E Goldberg
Journal:  Proc Natl Acad Sci U S A       Date:  1977-02       Impact factor: 11.205

3.  A proton-magnetic-resonance study of hydrogen-exchange reactions of yeast tryptophan synthase.

Authors:  C J Bailey; J P Malthouse
Journal:  Biochem J       Date:  1991-02-01       Impact factor: 3.857

4.  Interspecies hybrid tryptophan synthase-modified beta 2 protein formed from separate folding regions of the beta monomer.

Authors:  V Rocha; E F Brennan
Journal:  J Bacteriol       Date:  1980-05       Impact factor: 3.490

5.  Heme regulation of human cystathionine beta-synthase activity: insights from fluorescence and Raman spectroscopy.

Authors:  Colin L Weeks; Sangita Singh; Peter Madzelan; Ruma Banerjee; Thomas G Spiro
Journal:  J Am Chem Soc       Date:  2009-09-09       Impact factor: 15.419

  5 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.