Article
Quaternary structure sensitive tyrosine interactions in hemoglobin: a UV resonance Raman study of the double mutant rHb (beta99Asp-->Asn, alpha42Tyr-->Asp).
Biochemistry - 20 May 1997
Huang S, Peterson E S, Ho C, Friedman J M
Abstract excerpt
Two interactions involving tyrosines have been implicated in the communication pathway that links ligand binding to quaternary state changes in hemoglobin. Tyr alpha(1)42 stabilizes the alpha1beta2 T state interface through the formation of a hydrogen bond to Asp beta(2)99. The side chains of the penultimate Tyr residues (alpha140 and beta145) occupy the pockets made by helicies F and H in the deoxy form with the...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.