Protein dynamics by solid-state NMR: aromatic rings of the coat protein in fd bacteriophage.
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.
D003090:Coliphages / Q000032:analysis*; D009682:Magnetic Resonance Spectroscopy; D010649:Phenylalanine / Q000032:analysis; D011487:Protein Conformation; D014364:Tryptophan / Q000032:analysis; D014443:Tyrosine / Q000032:analysis; D014764:Viral Proteins
D014764:Viral Proteins; D014443:Tyrosine; D010649:Phenylalanine; D014364:Tryptophan