Ontology highlight
ABSTRACT:
SUBMITTER: Williams JK
PROVIDER: S-EPMC4674322 | biostudies-literature | 2015 Nov
REPOSITORIES: biostudies-literature
Williams Jonathan K JK Schmidt-Rohr Klaus K Hong Mei M
Solid state nuclear magnetic resonance 20150914
The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, have strongly overlapping (13)C chemical shift ranges between 100 and 160ppm, and have so far been largely neglected in solid-state NMR determination of protein structures. Yet aromatic residues play important roles in biology through π-π and cation-π interactions. To better resolve and assign aromatic residues' (13)C signals in magic-angle-spinning (MAS) solid-state NMR spectra, we introduce tw ...[more]