Selectivity of Tryptophan Residues in Mediating Photolysis of Disulfide Bridges in Goat α-Lactalbumin †
✍ Scribed by Vanhooren, A.; De Vriendt, K.; Devreese, B.; Chedad, A.; Sterling, A.; Van Dael, H.; Van Beeumen, J.; Hanssens, I.
- Book ID
- 126916481
- Publisher
- American Chemical Society
- Year
- 2006
- Tongue
- English
- Weight
- 226 KB
- Volume
- 45
- Category
- Article
- ISSN
- 0006-2960
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## Abstract Effects of deuteration on the Raman spectrum of a tryptophan residue have been examined. The 1386 cm^−1^ line of deuterated tryptophan residue has been found to be useful for tracing the hydrogen‐deuterium exchange reaction of this residue in a protein. An examination on bovine α‐lactal
The effect of Ca" ion on structural fluctuation of a milk Ca2+-binding protein, a-lactalbumin, under native conditions was investigated by comparing hydrogen-exchange reactions of tryptophan residues in the apo-form without Ca2+ and in the holo-form at 1 mM CaCl, at pH 7.0 in the presence of 0.1M Na