Life Sciences
New life sciences research from Carnegie Mellon University, Department of Biological Sciences outlined
Published in Medical Devices and Surgical Technology Week, June 8th, 2008
A new study, 'Effector-induced structural fluctuation regulates the ligand affinity of an allosteric protein: binding of inositol hexaphosphate has distinct dynamic consequences for the T and R States of hemoglobin,' is now available. "The present study reports distinct dynamic consequences for the T-and R-states of human normal adult hemoglobin (Hb A) due to the binding of a heterotropic allosteric effector, inositol hexaphosphate (IHP). A nuclear magnetic resonance (NMR) technique based on modified transverse relaxation optimized spectroscopy (TROSY) has been used to investigate the effect of conformational exchange of Hb A in both deoxy and CO forms, in the absence and presence of IHP,...
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