Role of Disulfide Bonds in Modulating Internal Motions of Proteins to Tune Their Function: Molecular Dynamics Simulation of Scorpion Toxin Lqh Iii.
From: Department of Biophysics, Faculty of Science, Tarbiat Modarres University, Tehran, Iran.
Proteins
- Publish Date: Apr 2006
- ISSN: 1097-0134
- Volume: 63
- Issue: 1
- Pages: 188-96
- Medium: Internet
- Language: English
- Citation (JAMA): Moghaddam Majid Erfani, Naderi-Manesh Hossein, et al. Role of Disulfide Bonds in Modulating Internal Motions of Proteins to Tune Their Function: Molecular Dynamics Simulation of Scorpion Toxin Lqh Iii.. Proteins Apr 2006;63:188-96
Abstract
A series of 1-ns MD simulations were performed on the scorpion toxin Lqh III in native and disulfide bond broken states. The removal of disulfide bonds has caused hydrogen bond network alteration in the five-residue turn, the long loop, the alpha-helix, the loop connecting strands II and III, and the C-terminal region. In addition and more importantly, it has influenced the amplitude of the fluctuations of five-residue turn, loops, and C-terminal region with a minor effect on the fluctuations of the cysteines in the broken bond sites. These findings suggest that disulfide bonds are not the most important factors in rigidifying their own locations, while they have more important effects at a global scale. Furthermore, our results reveal that disulfide bonds have considerable influence on the functionally important essential modes of motions and the correlations between the motions of the binding site residues. Therefore, we can conclude that disulfide bonds have a crucial role in modulating the function via adjusting the dynamics of scorpion toxin molecules. Although this conclusion cannot be generalized to all peptides and proteins, it demonstrates the importance of more investigations on this aspect of disulfide bond efficacy.
Mesh Headings (Keywords): Animals, Binding Sites, Computer Simulation, Databases, Protein, Disulfides, Hydrogen Bonding, Kinetics, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Conformation, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Proteins, Proteomics, Scorpion Venoms, Software, Toxins, Biological
Check for Full Text / PubMed Unique Identifier (PMID): 16400645
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.