Experimental pK_a Value Determination of All Ionizable Groups of a Hyperstable Protein.

ABSTRACT: Electrostatic interactions significantly contribute to the stability and function of proteins. The stabilizing or destabilizing effect of local charge is reflected in the perturbation of the pK_a value of an ionizable group from the intrinsic pK_a value. Herein, the charge network of a hyperstable dimeric protein (ribbon-helix-helix (rhh) protein from plasmid pRN1 from Sulfolobus islandicus) is studied through experimental determination of the pK_a values of all ionizable groups. Transitions were monitored by multiple NMR signals per ionizable group between pH 0 and 12.5, prior to a global analysis, which accounted for the effects of neighboring residues. It is found that for several residues involved in salt bridges (four Asp and one Lys) the pK_a v

SUBMITTER: Raum HN 

PROVIDER: S-EPMC6619245 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature