Construct optimization for protein NMR structure analysis using amide hydrogen/deuterium exchange mass spectrometry.

ABSTRACT: Disordered or unstructured regions of proteins, while often very important biologically, can pose significant challenges for resonance assignment and three-dimensional structure determination of the ordered regions of proteins by NMR methods. In this article, we demonstrate the application of (1)H/(2)H exchange mass spectrometry (DXMS) for the rapid identification of disordered segments of proteins and design of protein constructs that are more suitable for structural analysis by NMR. In this benchmark study, DXMS is applied to five NMR protein targets chosen from the Northeast Structural Genomics project. These data were then used to design optimized constructs for three partially disordered proteins. Truncated proteins obtained by deletion of disordered N- and C-terminal tails were evalu

SUBMITTER: Sharma S 

PROVIDER: S-EPMC2739808 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature