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Raman spectroscopic analysis of the secondary structure in Panulirus interruptus hemocyanin
Author(s) -
Williams Robert W.,
Hendrickson Wayne A.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80173-8
Subject(s) - hemocyanin , raman spectroscopy , protein secondary structure , chemistry , analytical chemistry (journal) , amide , crystallography , biology , chromatography , biochemistry , physics , optics , genetics , antigen
The secondary structure content of Panulirus interruptus hemocyanin crystals is estimated to be 29±5% helix and 42±4% ß‐strand. These estimates are obtained from an analysis of the Raman amide I spectrum. This report constitutes a test of this method of analyzing Raman spectra since the X‐ray structure of P. interruptus, which is unknown to us, is under intensive study. Also, the amide I spectrum of P. interruptus in solution, at a somewhat higher pH, is significantly different from the spectrum of crystals which indicates that the secondary structure content may be different in the solution sample.