Literature DB >> 5036166

Magnetic resonance studies of protein-small molecule interactions. Binding of N-trifluoroacetyl-D-(and L-)-p-fluorophenylalanine to -chymotrypsin.

K L Gammon, S H Smallcombe, J H Richards.   

Abstract

Entities:  

Mesh：

Substances：

Year:  1972        PMID： 5036166     DOI： 10.1021/ja00768a027

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN： 0002-7863            Impact factor:   15.419


× No keyword cloud information.
  4 in total

Review 1.  Use of 19F NMR to probe protein structure and conformational changes.

Authors:  M A Danielson; J J Falke
Journal:  Annu Rev Biophys Biomol Struct       Date:  1996

2.  Structure and dynamics of alpha-chymotrypsin-N-trifluoroacetyl-4-fluorophenylalanine complexes.

Authors:  A R Jacobson; J T Gerig
Journal:  J Biomol NMR       Date:  1991-07       Impact factor: 2.835

3.  Attractant- and disulfide-induced conformational changes in the ligand binding domain of the chemotaxis aspartate receptor: a 19F NMR study.

Authors:  M A Danielson; H P Biemann; D E Koshland; J J Falke
Journal:  Biochemistry       Date:  1994-05-24       Impact factor: 3.162

4.  Activation of the phosphosignaling protein CheY. I. Analysis of the phosphorylated conformation by 19F NMR and protein engineering.

Authors:  S K Drake; R B Bourret; L A Luck; M I Simon; J J Falke
Journal:  J Biol Chem       Date:  1993-06-25       Impact factor: 5.157
  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.