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Infrared absorption of tyrosine side chains in proteins
Author(s) -
Bendit E. G.
Publication year - 1967
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1967.360050607
Subject(s) - tyrosine , chemistry , residue (chemistry) , side chain , infrared , infrared spectroscopy , absorption (acoustics) , deuterium , absorption band , biochemistry , organic chemistry , optics , polymer , physics , quantum mechanics
Poly‐ L ‐tyrosine absorbs strongly at 1515 cm. −1 , and a band at this frequency has been found in a number of proteins and has been assigned to the tyrosine residue. The assignment was confirmed by examination of spectra of deuterated proteins, which usually exhibit a residual band at 1513 cm. −1 . In proteins, this band correlates linearly with known tyrosine content, but the point corresponding to poly‐ L ‐tyrosine itself does not fall on the correlation line. The possibility and limitations of using the infrared method for tyrosine determinations is discussed.