%0 Journal Article %1 gall_protein_1982 %A Gall, C M %A Cross, T A %A DiVerdi, J A %A Opella, S J %D 1982 %J Proc. Natl. Acad. Sci. U.S.A. %K Coliphages,Magnetic Conformation,Tryptophan,Tyrosine,Viral Proteins Resonance Spectroscopy,Phenylalanine,Protein %N 1 %P 101--105 %T Protein dynamics by solid-state \NMR\: aromatic rings of the coat protein in fd bacteriophage %V 79 %X 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.

@article{gall_protein_1982, 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.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {Gall, C M and Cross, T A and DiVerdi, J A and Opella, S J}, biburl = {https://www.bibsonomy.org/bibtex/2bb8d0b0f44ddabcd3d9716543755d6e2/nmrresource}, interhash = {22c3096e4883c757330ae913a92cb4be}, intrahash = {bb8d0b0f44ddabcd3d9716543755d6e2}, issn = {0027-8424}, journal = {Proc. Natl. Acad. Sci. U.S.A.}, keywords = {Coliphages,Magnetic Conformation,Tryptophan,Tyrosine,Viral Proteins Resonance Spectroscopy,Phenylalanine,Protein}, month = jan, number = 1, pages = {101--105}, pmid = {6948294}, shorttitle = {Protein dynamics by solid-state {\{}NMR{\}}}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{Protein dynamics by solid-state {\{}NMR{\}}: aromatic rings of the coat protein in fd bacteriophage}}, volume = 79, year = 1982 }