Contribution of side-chain chromophores to the optical activity of proteins: Model compound studies. I. α-Methyl-L-tyrosine
✍ Scribed by Warren J. Goux; Dennis B. Cooke; Raquel E. Rodriguez; Thomas M. Hooker Jr.
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1974
- Tongue
- English
- Weight
- 850 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
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.