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. 1982 Jan;79(1):101-5.
doi: 10.1073/pnas.79.1.101.

Protein dynamics by solid-state NMR: aromatic rings of the coat protein in fd bacteriophage

C M Gall, T A Cross, J A DiVerdi, S J Opella

Protein dynamics by solid-state NMR: aromatic rings of the coat protein in fd bacteriophage

C M Gall et al. Proc Natl Acad Sci U S A. 1982 Jan.

Abstract

The motions of the aromatic amino acids of the fd bacteriophage coat protein are described by solid-state 2H, 13C, and 15N NMR. Tryptophan-26 is immobile on time scales as slow as 10(3) HZ. The phenylalanine and tyrosine rings undergo 180 degree flips about the C beta--C gamma bond axis more often than 10(6) HZ as well as small-amplitude rapid motions in other directions.

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References

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