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. © 1993, Elsevier B.V. All rights reserved.
Probing Conformational Transitions in Interface α1β2 of Human Hemoglobin by Site-Directed Mutagenesis / Vallone, B.; Cavalli, V.; Brunori, M.. - 47:C(1993), pp. 505-509. [10.1016/B978-0-444-89372-7.50066-X]
Probing Conformational Transitions in Interface α1β2 of Human Hemoglobin by Site-Directed Mutagenesis
Vallone B.;
1993
Abstract
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. © 1993, Elsevier B.V. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
