Study of the structural environment of DsbA protein by labeling of tryptophan analogs

Progress in Biochemistry and Biophysics

Volumn 29, Issue 2, 2002, Pages 319-322

  Li, Qi ^a   Hu, Hong Yu ^a   Sheng, Wan Yun ^a   Zhao, Xin Yan ^a   Xu, Gen Jun ^a  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

Author keywords

19F NMR; Biosynthetic labeling; DsbA protein; Fluorescence; Structural environment

Indexed keywords

PROTEIN; PROTEIN DSBA; TRYPTOPHAN DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; FLUORESCENCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION REDUCTION REACTION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE;

EID: 0036525560     PISSN: 10003282     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (7)

1. Time-resolved fluorescence spectroscopy
2. 19F NMR to probe protein structure and conformational changes
3. Crystal structures of reduced and oxidized DsbA: Investigation of domain motion and thiolate stabilization
4. Study of the redox properties of metallothionein in vitro by reacting with DsbA protein
5. Incorporation of tryptophan analogues into staphylococcal nuclease, its V66W mutant, and ΔA137-149 fragment: Spectroscopic studies
6. Brightness speeds search for structures great and small
7. Preparation of selenomethionyl proteins for phase determination