Amino acid selective unlabeling for sequence specific resonance assignments in proteins.

ABSTRACT: Sequence specific resonance assignment constitutes an important step towards high-resolution structure determination of proteins by NMR and is aided by selective identification and assignment of amino acid types. The traditional approach to selective labeling yields only the chemical shifts of the particular amino acid being selected and does not help in establishing a link between adjacent residues along the polypeptide chain, which is important for sequential assignments. An alternative approach is the method of amino acid selective 'unlabeling' or reverse labeling, which involves selective unlabeling of specific amino acid types against a uniformly (13)C/(15)N labeled background. Based on this method, we present a novel approach for sequential assignments in proteins. The method involve

SUBMITTER: Krishnarjuna B 

PROVIDER: S-EPMC3020294 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature