Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity.

ABSTRACT: The Gibbs free energy difference between native and unfolded states ("stability") is one of the fundamental characteristics of a protein. By exploiting the thermodynamic linkage between ligand binding and stability, interactions of a protein with small molecules, nucleic acids, or other proteins can be detected and quantified. Determination of protein stability can therefore provide a universal monitor of biochemical function. Yet, the use of stability measurements as a functional probe is underutilized, because such experiments traditionally require large amounts of protein and special instrumentation. Here we present the quantitative cysteine reactivity (QCR) technique to determine protein stabilities rapidly and accurately using only picomole quantities of material and readily accessibl

SUBMITTER: Isom DG 

PROVIDER: S-EPMC2841886 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature