Membrane protein structural validation by oriented sample solid-state NMR: diacylglycerol kinase.

ABSTRACT: The validation of protein structures through functional assays has been the norm for many years. Functional assays perform this validation for water-soluble proteins very well, but they need to be performed in the same environment as that used for the structural analysis. This is difficult for membrane proteins that are often structurally characterized in detergent environments, although functional assays for these proteins are most frequently performed in lipid bilayers. Because the structure of membrane proteins is known to be sensitive to the membrane mimetic environment, such functional assays are appropriate for validating the protein construct, but not the membrane protein structure. Here, we compare oriented sample solid-state NMR spectral data of diacylglycerol kinase previously pu

SUBMITTER: Murray DT 

PROVIDER: S-EPMC4008839 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature