𝔖 Bobbio Scriptorium
✦   LIBER   ✦

An investigation of the electronic environment of tryptophan in proteins: Reliability of fluorescence quenching experiments

✍ Scribed by Fernanda Ricchelli


Publisher
Elsevier Science
Year
1990
Tongue
English
Weight
611 KB
Volume
7
Category
Article
ISSN
1011-1344

No coin nor oath required. For personal study only.


πŸ“œ SIMILAR VOLUMES


The Effects of Biological Environments o
✍ Dr. Xiaohua Chen; Hongjing Dai; Dr. Jilai Li; Prof. Xuri Huang; Prof. Zidong Wei πŸ“‚ Article πŸ“… 2011 πŸ› John Wiley and Sons 🌐 English βš– 851 KB

## Abstract Clarifying the contribution of tryptophan (Trp) to electron‐transfer (ET) processes in different protein surroundings can help to understand the effective pathway of ET in proteins. Interactions between Trp residues and protein microsurroundings involve intermolecular H‐bonds, cation an

Fluorescence quenching in the DsbA prote
✍ Alain Sillen; Jens Hennecke; Daniela Roethlisberger; Rudi Glockshuber; Yves Enge πŸ“‚ Article πŸ“… 1999 πŸ› John Wiley and Sons 🌐 English βš– 253 KB πŸ‘ 2 views

The disulfide oxidoreductase DsbA is a strong oxidant of protein thiols and is required for efficient disulfide bond formation in the bacterial periplasm. DsbA contains two tryptophans: W76 and W126. The fluorescence of W76 changes upon reduction of the disulfide bridge, as analyzed previously (Henn

Probing local environments of tryptophan
✍ Jennifer Zemsky; Elena Rusinova; Yale Nemerson; Linda A. Luck; J.B. Alexander Ro πŸ“‚ Article πŸ“… 1999 πŸ› John Wiley and Sons 🌐 English βš– 165 KB πŸ‘ 1 views

19 F nuclear magnetic resonance ( 19 F NMR) of 5-fluorotryptophan (5F-Trp) and tryptophan (Trp) fluorescence both provide information about local environment and solvent exposure of Trp residues. To compare the information provided by these spectroscopies, the four Trp residues in recombinant solubl