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

Proc Natl Acad Sci U S A. 1982 Jan;79(1):101-5. doi: 10.1073/pnas.79.1.101.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Coliphages / analysis*
  • Magnetic Resonance Spectroscopy
  • Phenylalanine / analysis
  • Protein Conformation
  • Tryptophan / analysis
  • Tyrosine / analysis
  • Viral Proteins*

Substances

  • Viral Proteins
  • Tyrosine
  • Phenylalanine
  • Tryptophan