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Conformational studies of proteins with aromatic side‐chain effects
Author(s) -
Goodman Murray,
Toniolo Claudio
Publication year - 1968
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.1968.360061202
Subject(s) - chemistry , side chain , chromophore , circular dichroism , optical rotatory dispersion , aromatic amino acids , absorption (acoustics) , ultraviolet , peptide , amide , crystallography , photochemistry , stereochemistry , amino acid , organic chemistry , polymer , biochemistry , optics , physics
We present here a brief analysis of ultraviolet isotropic absorption and related circular dichroism of the n –π* and π–π* transitions for the peptide (amide) chromophore in the 185–240 mμ region. Investigations by ultraviolet absorption and circular dichroism techniques on natural amino acids with aromatic chromophores in their side chains are also reported. By taking into account both the peptide and aromatic transitions we discuss the conformational studies of proteins with aromatic side‐chain effects. Our attention is largely focused on the optical rotatory dispersion and circular dichroism spectra of these proteins in the near ultraviolet region, where characteristic aromatic side‐chain bands occur. The 185–240 mμ region is also discussed when evidence exists of overlapping Cotton effects of aromatic and peptide groups.