Article
Mutational effects at the subunit interfaces of human hemoglobin: evidence for a unique sensitivity of the T quaternary state to changes in the hinge region of the alpha 1 beta 2 interface.
Biochemistry - 16 Oct 2001
Noble R W, Hui H L, Kwiatkowski L D, Paily P, DeYoung A, Wierzba A, Colby J E, Bruno S, Mozzarelli A
Abstract excerpt
A set of variant human hemoglobins, each with an Ala or Gly substitution at a single residue, has been prepared, and the kinetics of their reactions with carbon monoxide have been measured. This reaction is rate-limited by the binding of the first CO to the deoxygenated T state of the protein. The magnitudes of the effects of the mutations on CO combination vary widely, and, with the exception of beta Y145, the...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.