Allosteric transitions of proteins studied by topological networks: a preliminary investigation on human hemoglobin.

Authors

  • Caruso Lisa Beatrice Sapienza, University of Rome
  • Alessandro Giuliani Istituto Superio di Sanità
  • Alfredo Colosimo Sapienza - University of Rome

Keywords:

Topological Networks, Hemoglobin, Allostery

Abstract

A concise description of the 3D structure of a and b chains of human haemoglobin, as well as of ab dimers, is provided for both the R and T forms on the basis of topological network parameters. Such parameters are able to account for the allosteric conformational transitions as derived by standard 3D pictures and models in the literature. In particular, the difference between the R and T forms appears more relevant in the case of dimers, in agreement with the idea that dimers are essential in the allosteric mechanism of Hb as an oxygen carrier.This result encourages the extension of the network-based, topological representation of protein structures to less overexploited systems than Hb, as well as to the vast realm of data coming from resonance spectroscopy.

Author Biographies

Caruso Lisa Beatrice, Sapienza, University of Rome

Dept. SAIMLAL

Alessandro Giuliani, Istituto Superio di Sanità

Dept. of Environment and Health

Alfredo Colosimo, Sapienza - University of Rome

Dept. SAIMLAL

Downloads

How to Cite

Beatrice, C. L., Giuliani, A., & Colosimo, A. (2012). Allosteric transitions of proteins studied by topological networks: a preliminary investigation on human hemoglobin. Biophysics and Bioengineering Letters, 5(1). Retrieved from https://rosa.uniroma1.it/rosa00/index.php/biophysics_and_bioengineering/article/view/10475

Issue

Section

Section 1: Regular papers

Most read articles by the same author(s)

1 2 > >>