December 2017 issue
The yield of protein refolding is reciprocal to the number of proline residues in the target protein. Hydrogen bonds are the primary driving force for de novo protein folding
The switch I region in G12A K-Ras undergoes a significant reorganization that results in new interactions between GTP and Tyr32 that stabilize the precatalytic state. These new interactions cause the reduced intrinsic GTP-hydrolysis rate of the G12A K-Ras mutant.
Homology-independent methods for ab initio phasing of α-helical transmembrane proteins are explored.
A standardized technique for high-pressure cooling of protein crystals has been developed that encompasses all steps from crystal retrieval to automated mounting of the sample at the synchrotron. A wide chemical space for sample cooling has been tested. Amorphous ice was formed in more than 89% of the solutions.
The structures of biphenyl synthase, of biphenyl synthase complexed with benzoyl-CoA and of benzophenone synthase are compared with that of a chalcone synthase homolog. These structures reveal that benzoic acid-specific type III polyketide synthases contain distinct structural elements, including a novel pocket, which underlie their evolutionary emergence.
An interaction-based fragmentation scheme for solving the issue of scalability in quantum refinement has been developed, implemented in the Q|R software and validated on an amyloid cross-β spine (PDB entry 2oNA).