Measurement of histidine pKa values and tautomer populations in invisible protein states.

ABSTRACT: The histidine imidazole side chain plays a critical role in protein function and stability. Its importance for catalysis is underscored by the fact that histidines are localized to active sites in ∼ 50% of all enzymes. NMR spectroscopy has become an important tool for studies of histidine side chains through the measurement of site-specific pK(a)s and tautomer populations. To date, such studies have been confined to observable protein ground states; however, a complete understanding of the role of histidine electrostatics in protein function and stability requires that similar investigations be extended to rare, transiently formed conformers that populate the energy landscape, yet are often "invisible" in standard NMR spectra. Here we present NMR experiments and a simple strategy for studi

SUBMITTER: Hansen AL 

PROVIDER: S-EPMC4035968 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature