Carbon and amide detect backbone assignment methods of a novel repeat protein from the staphylocoagulase in S. aureus.

ABSTRACT: The C-terminal repeat domain of staphylocoagulase that is secreted by the S. aureus is believed to play an important role interacting with fibrinogen and promotes blood clotting. To study this interaction by NMR, full assignment of each amide residue in the HSQC spectrum was required. Despite of the short sequence of the repeat construct, the HSQC spectrum contained a substantial amount of overlapped and exchange broadened resonances, indicating little secondary or tertiary structure. This caused severe problems while using the conventional, amide based NMR method for the backbone assignment. With the growing interest in small apparently disordered proteins, these issues are being faced more frequently. An alternative strategy to improve the backbone assignment capability involved carbon d

SUBMITTER: Voehler M 

PROVIDER: S-EPMC6057470 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature