alexa MD Simulation Studies of Fumarase Reveal Thermo Dynamic
ISSN: 2161-0398

Journal of Physical Chemistry & Biophysics
Open Access

Like us on:
OMICS International organises 3000+ Global Conferenceseries Events every year across USA, Europe & Asia with support from 1000 more scientific Societies and Publishes 700+ Open Access Journals which contains over 50000 eminent personalities, reputed scientists as editorial board members.

Open Access Journals gaining more Readers and Citations

700 Journals and 15,000,000 Readers Each Journal is getting 25,000+ Readers

This Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)

Short Communication

MD Simulation Studies of Fumarase Reveal Thermo Dynamical Stability

Salam Pradeep Singh1*, Chitta Ranjan Deb2, Lakhmi Nandan Kakati3 and Bolin Kumar Konwar4
1Bioinformatics Infrastructure Facility, Nagaland University, Lumami 798627, Nagaland, India
2Department of Botany, Nagaland University, Lumami 798627, Nagaland, India
3Department of Zoology, Nagaland University, Lumami 798627, Nagaland, India
4Department of Molecular Biology and Biotechnology, Tezpur University, Tezpur 784028, Assam, India
Corresponding Author : Salam Pradeep Singh
Bioinformatics Infrastructure Facility
Nagaland University, Lumami-798 627
Nagaland, India
Tel: +918486268935
E-mail: [email protected]
Received: February 15, 2016 Accepted: February 24, 2016 Published: February 29, 2016
Citation: Singh SP, Deb CR, Kakati LN, Konwar BK (2016) MD Simulation Studies of Fumarase Reveal Thermo Dynamical Stability. J Phys Chem Biophys 6:206. doi:10.4172/2161-0398.1000206
Copyright: © 2016 Singh SP, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


Fumarase enzyme is known to catalyse the stereo specific inter conversion of fumarate to L-malate which is a part of the Krebs cycle. Despite the biological significance and importance of this enzyme, the reaction mechanism of fumarase is not completely understood or known. In this context an experiment on molecular dynamics simulation was carried out for at least 10 nanoseconds molecular dynamics simulation run using Nano Scale Molecular Dynamics program implemented in Discovery Studio 4.0. The trajectory analysis of various energy parameters revealed the thermo dynamical stability of the enzyme. The present findings may aid in understanding the biological significance of this enzyme.


Share This Page

Additional Info

Loading Please wait..
Peer Reviewed Journals
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version