new sequential model for human hemoglobin: alpha subunit as cooperativity inducer

Authors

mohammad reza dayer

mohammad saaid dayer

bahador taheri

abstract

hemoglobin is a tetrameric oxygen transport protein in animal bodies. however, there is a paucity of information regarding differences between alpha and beta subunits of hemoglobin in terms of oxygen affinity. the sequential model of koshland, nemthy and filmer (knf model) has attributed similar affinities to both alpha and beta subunits. the main purpose of the present study is to construct a new sequential model for hemoglobin oxygenation based on higher oxygen affinities for alpha subunits. to this end, coordinate files of 19 oxy and 41 deoxy hemoglobin structures were used as starting structures. these files were processed using microsoft excel and spss software in order to calculate euclidean distances between each pair of proximal and distal histidine fe2+ as well as other pairs of atoms of interest. the calculated distances were then compared for either set of hemoglobin conformations, i.e. oxy and deoxy conformations. our results showed that α2 subunit show higher structural changes that could be related to oxygen affinity. this subunit could be introduced as initiator of hemoglobin oxygenation and cooperativity. subunit α2 in our sequential model induces relaxed conformation in α1, β2 and β1 respectively. the order of oxygen affinity in our model is as follow: α2 > α1 > β1 > β2.

Upgrade to premium to download articles

Sign up to access the full text

Already have an account?login

similar resources

New Sequential Model for Human Hemoglobin: Alpha Subunit as Cooperativity Inducer

Hemoglobin is a tetrameric oxygen transport protein in animal bodies. However, there is a paucity of information regarding differences between alpha and beta subunits of hemoglobin in terms of oxygen affinity. The sequential model of Koshland, Nemthy and Filmer (KNF model) has attributed similar affinities to both alpha and beta subunits. The main purpose of the present study is to construct a ...

full text

Structure-specific model of hemoglobin cooperativity.

A generalization of the Szabo-Karplus statistical mechanical model for hemoglobin cooperativity is formulated. The model fits the available thermodynamic and spectroscopic data with assumptions that are consistent with structural results and empirical energy function calculations. It provides a mechanism of hemoglobin cooperativity that is a generalization of the proposals of Monod, Wyman, and ...

full text

O-11: Immunoneutralization of Inhibin Alpha Subunit as A Tool for Improving Farm Animal Fertility

Background: The objectives of a series of studies undertaken was to improve farm animal reproductive efficiency in terms of embryo production efficiency, conception rate and litter size by immunoneutralization of inhibin in conjunction with other conventional reproductive techniques. Materials and Methods: A recombinant porcine inhibin alpha-subunit mature peptide was produced by mass scale and...

full text

A tri state mechanism for oxygen release in fish hemoglobin: Using Barbus sharpeyi as a model

Hemoglobin is a porphyrin containing protein with an a2b2 tetrameric structure and like other porphyrin compounds shows spectral behavior of species specific characteristics. Researchers tend to relate bands in the hemoglobin spectra to certain structural and/or functional features. Given the fact that hemoglobin is the main oxygen carrier in animals functioning through the Oxy«Deoxy equilibriu...

full text

Unraveling subunit cooperativity in homotetrameric HCN2 channels.

In a multimeric receptor protein, the binding of a ligand can modulate the binding of a succeeding ligand. This phenomenon, called cooperativity, is caused by the interaction of the receptor subunits. By using a complex Markovian model and a set of parameters determined previously, we analyzed how the successive binding of four ligands leads to a complex cooperative interaction of the subunits ...

full text

My Resources

Save resource for easier access later


Journal title:
biomacromolecular journal

Publisher: iran society of biophysical chemistry (isobc)

ISSN

volume 1

issue 2 2015

Hosted on Doprax cloud platform doprax.com

copyright © 2015-2023