© 2015. Maryam Ghadamgahi & Davood Ajloo. This is a research/review paper, distributed under the terms of the Creative
Commons Attribution-Noncommercial 3.0 Unported License http://creativecommons.org/licenses/by-nc/3.0/), permitting all non-
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Global Journal of Researches in Engineering: C
Chemical Engineering
Volume 15 Issue 3 Version 1.0 Year 2015
Type: Double Blind Peer Reviewed International Research Journal
Publisher: Global Journals Inc. (USA)
Online ISSN: 2249-4596 & Print ISSN: 0975-5861
Influence of Scan Rate on Simulation of Differential Scanning
Calorimetry Profiles of Protein Denaturationt
By Maryam Ghadamgahi & Davood Ajloo
Damghan University, Iran
Abstract- The heat capacity has played a major role in proteins. Its calculation by atomistic
simulation methods remains a significant challenge due to the complex and dynamic nature of
protein structures and this work compares the denaturation effect of bovine carbonic anhydrase
(BCA) by heat, pH and scan rate dependence of protein denaturation by molecular dynamics
(MD) simulation. To better understand this factor on calculating a protein heat capacity and T
m
,
we have provided a comparative analysis of simulation models that differ in their scan rate and
pH description. Our model protein system is the carbonic anhydrase, and a series of 20 ns
simulated DSC with different scan rate (v= 0.10, 0.0125, 0.015 and 0.02 K/ps) and pH have been
reported by simulated annealing performed at temperatures ranging from 250 to 575 K, starting
from the carbonic anhydrase native structure. It was observed that, our systems were quite
sensitive to the description and the calculated melting temperature (T
m
) varied in the range 353-
438 K and was higher for higher scan rates systems and lower for acidic condition.
Keywords: carbonic anhydrase, melting temperature, molecular dynamics simulation, scan rate,
simulated annealing.
GJRE-C Classification: FOR Code: 030599, 030505
InfluenceofScanRateonSimulationofDifferentialScanningCalorimetryProfilesofProteinDenaturationt
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