Tehran University of Medical Sciences

Science Communicator Platform

Stay connected! Follow us on X network (Twitter):
Share this content! On (X network) By
Structural Stability of Myoglobin and Glycomyoglobin: A Comparative Molecular Dynamics Simulation Study Publisher Pubmed



Alizadehrahrovi J1 ; Shayesteh A1 ; Ebrahimhabibi A2, 3
Authors
Show Affiliations
Authors Affiliations
  1. 1. School of Chemistry, College of Science, University of Tehran, Tehran, Iran
  2. 2. Biosensor Research Center, Endocrinology and Metabolism Molecular-Cellular Sciences Institute, Tehran University of Medical Sciences, Shariati Hospital, North Kargar Avenue, Tehran, 1411413137, Iran
  3. 3. Endocrinology and Metabolism Research Center, Endocrinology and Metabolism Clinical Sciences Institute, Tehran University of Medical Sciences, Tehran, Iran

Source: Journal of Biological Physics Published:2015


Abstract

Glycoproteins are formed as the result of enzymatic glycosylation or chemical glycation in the body, and produced in vitro in industrial processes. The covalently attached carbohydrate molecule(s) confer new properties to the protein, including modified stability. In the present study, the structural stability of a glycoprotein form of myoglobin, bearing a glucose unit in the N-terminus, has been compared with its native form by the use of molecular dynamics simulation. Both structures were subjected to temperatures of 300 and 500 K in an aqueous environment for 10 ns. Changes in secondary structures and RMSD were then assessed. An overall higher stability was detected for glycomyoglobin, for which the most stable segments/residues were highlighted and compared with the native form. The simple addition of a covalently bound glucose is suggested to exert its stabilizing effect via increased contacts with surrounding water molecules, as well as a different pattern of interactions with neighbor residues. © 2015, Springer Science+Business Media Dordrecht.