Titration of ionizable groups in proteins using multiple neutron data sets from a single crystal: application to the small GTPase Ras.

ABSTRACT: Neutron protein crystallography (NPC) reveals the three-dimensional structures of proteins, including the positions of H atoms. The technique is particularly suited to elucidate ambiguous catalytic steps in complex biochemical reactions. While NPC uniquely complements biochemical assays and X-ray structural analyses by revealing the protonation states of ionizable groups at and around the active site of enzymes, the technique suffers from a major drawback: large single crystals must be grown to compensate for the relatively low flux of neutron beams. However, in addition to revealing the positions of hydrogens involved in enzyme catalysis, NPC has the advantage over X-ray crystallography that the crystals do not suffer radiation damage. The lack of radiation damage can be exploited to cond

SUBMITTER: Knihtila R 

PROVIDER: S-EPMC6360437 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature