Large Multidomain Protein NMR: HIV-1 Reverse Transcriptase Precursor in Solution.

ABSTRACT: NMR studies of large proteins, over 100 kDa, in solution are technically challenging and, therefore, of considerable interest in the biophysics field. The challenge arises because the molecular tumbling of a protein in solution considerably slows as molecular mass increases, reducing the ability to detect resonances. In fact, the typical 1H-13C or 1H-15N correlation spectrum of a large protein, using a 13C- or 15N-uniformly labeled protein, shows severe line-broadening and signal overlap. Selective isotope labeling of methyl groups is a useful strategy to reduce these issues, however, the reduction in the number of signals that goes hand-in-hand with such a strategy is, in turn, disadvantageous for characterizing the overall features of the protein. When domain motion exists in large prote

SUBMITTER: Ilina TV 

PROVIDER: S-EPMC7765405 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature