An enzymatic approach to the labeling of tryptophan residues in peptides and proteins
✍ Scribed by Alfred Maelicke; Detlef Krüger; Joseph Roberts; Henry Rosenfeld
- Book ID
- 115908649
- Publisher
- Elsevier Science
- Year
- 1978
- Tongue
- English
- Weight
- 400 KB
- Volume
- 85
- Category
- Article
- ISSN
- 0014-5793
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Fluorescence quenching is used to gain information on the exposure of tryptophan residues to lipid in membrane-bound proteins and peptides. A protocol is developed to calculate this exposure, based on a comparison of quenching efficiency and of a fluorescence lifetime (or quantum yield) measured for
L-[1.2-13C2, 15N]Serine was prepared from [1,2-13C2, 15N]glycine on a gram scale by the use of the enzyme serine hydroxymethyltransferase. The reaction was monitored by 13C-NMR spectroscopy. This is the first simultaneously 13C- and 15N-labelled serine isotopomer so far reported. Part of the product