| Literature DB >> 6948294 |
C M Gall, T A Cross, J A DiVerdi, S J Opella.
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.Entities:
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Year: 1982 PMID: 6948294 PMCID: PMC345669 DOI: 10.1073/pnas.79.1.101
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205