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Contribution of side‐chain chromophores to the optical activity of proteins: Model compound studies. I. α‐Methyl‐ L ‐tyrosine
Author(s) -
Goux Warren J.,
Cooke Dennis B.,
Rodriguez Raquel E.,
Hooker Thomas M.
Publication year - 1974
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.1974.360131113
Subject(s) - chemistry , chromophore , circular dichroism , tyrosine , side chain , molecule , stereochemistry , chirality (physics) , polymer , photochemistry , biochemistry , organic chemistry , nambu–jona lasinio model , chiral symmetry breaking , physics , quantum mechanics , quark
The optical rotatory power and the conformational energy of the amino acid α‐methyl‐ L ‐tyrosine has been calculated as a function of molecular conformation. Comparison of the results of these theoretical calculations with experimental circular dichroism data indicates that the conformational freedom of this molecule is highly restricted. The most heavily populated conformations appear to be those near χ1 = 60°, χ2 = 80°, Ψ = 175°, and χ1 = 300°, χ2 = 80°, Ψ = 5°. The χ1 = 180° conformations are not likely to be populated to a significant extent at ordinary temperatures.