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Raman spectroscopic study of the environment of tryptophan residues in bovine α-lactalbumin

✍ Scribed by H. Van Dael; E. Tieghem; F. Van Cauwelaert

Book ID
112977208
Publisher
Indian Academy of Sciences,Royal Society of Chemistry
Year
1990
Tongue
English
Weight
143 KB
Volume
102
Category
Article
ISSN
0253-4134

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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

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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