Mechanism of tertiary structural change in hemoglobin.
نویسندگان
چکیده
منابع مشابه
Direct observation of photolysis-induced tertiary structural changes in hemoglobin.
Human Hb, an alpha2beta2 tetrameric oxygen transport protein that switches from a T (tense) to an R (relaxed) quaternary structure during oxygenation, has long served as a model for studying protein allostery in general. Time-resolved spectroscopic measurements after photodissociation of CO-liganded Hb have played a central role in exploring both protein dynamical responses and molecular cooper...
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Hemoglobin variants in which a frameshift results in chain elongation are unusual. Hemoglobin Pakse (Hb Pakse) is an unstable hemoglobin with abnormal elongation, first described in Indochina. An alpha2-globin gene termination codon mutation, TAA -->TAT or Term -->Tyr, has been described in the pathogenesis of Hb Pakse. This abnormality causes a frameshift that elongates the alpha chain amino a...
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terms of address as an important linguistics items provide valuable information about the interlocutors, their relationship and their circumstances. this study was done to investigate the change route of persian address terms in the two recent centuries including three historical periods of qajar, pahlavi and after the islamic revolution. data were extracted from a corpus consisting 24 novels w...
15 صفحه اولApplication of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.
The transition state for the R in equilibrium with T quaternary conformational change of hemoglobin has thermodynamic properties much closer to those of the R conformation than to those of the T conformation. This finding is based on a comparison of activation and equilibrium enthalpy and entropy changes and on the observation of a linear free energy relationship between quaternary rate and equ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1977
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.74.3.801