Solvent saturation transfer to proteins (SSTP) for structural and functional characterization of proteins.

ABSTRACT: Protein structure determination using NMR is dependent on experimentally acquired distance restraints. Often, however, an insufficient number of these restraints are available for determining a protein's correct fold, much less its detailed three-dimensional structure. In consideration of this problem, we propose a simple means to acquire supplemental structural restraints from protein surface accessibilities using solvent saturation transfer to proteins (SSTP), based on the principles of paramagnetic chemical-exchange saturation transfer. Here, we demonstrate the utility of SSTP in structure calculations of two proteins, TSG101 and ubiquitin. The observed SSTP was found to be directly proportional to solvent accessibility. Since SSTP does not involve the direct excitation of water, which

SUBMITTER: Mishra P 

PROVIDER: S-EPMC5820130 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature