Aiming at the study of the effect of Trp at the α1β2 interface of hemoglobin A (=Hb) on the stability of the tetrameric form of this protein and in order to introduce an additional probe for the T->R conformational transition, we have modelled by computer and produced in E. coli three Hb mutants: β37Trp->Thr, β37Trp->Thr/ α38Thr->Trp and α38Thr->Trp. An increase in the spectroscopic transition attributed to a Trp in the α1β2 interface of Hb was observed and a variation of the tetramer<->dimer equilibrium of the hemoglobin mutants was observed. The second observation is consistent with the behaviour expected from molecular modelling computations.

Original languageEnglish
Title of host publicationStudies in Organic Chemistry
Number of pages5
StatePublished - Jan 1 1993

Publication series

NameStudies in Organic Chemistry
ISSN (Print)0165-3253


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