Direct observation of conformational population shifts in crystalline human hemoglobin.

ABSTRACT: Although X-ray crystallography is the most commonly used technique for studying the molecular structure of proteins, it is not generally able to monitor the dynamic changes or global domain motions that often underlie allostery. These motions often prevent crystal growth or reduce crystal order. We have recently discovered a crystal form of human hemoglobin that contains three protein molecules allowed to express a full range of quaternary structures, whereas maintaining strong X-ray diffraction. Here we use this crystal form to investigate the effects of two allosteric effectors, phosphate and bezafibrate, by tracking the structures and functions of the three hemoglobin molecules following the addition of each effector. The X-ray analysis shows that the addition of either phosphate or bez

SUBMITTER: Shibayama N 

PROVIDER: S-EPMC5672048 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature