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Research Paper | May 1, 2013

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Molecular mechanic and monte carlo study of polymorphism effects on biophysical chemistry properties of XRCC1 BRCT2 domain

Jamshid Mehrzad, Majid Monajjemi, Mohammad Hashemi, Hamidreza Sima

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J. Bio. Env. Sci.3(5), 102-107, May 2013

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Abstract

DNA repair is one of the most important process that maintains genomic integrity and cell survival. X-ray repair cross-complementing group 1 (XRCC1) is one of proteins that involves in this process. XRCC1 encompasses two BRCT domains (BRCT1and BRCT2). Any change in XRCC1 residues can alter function and its stability. One of the normal substitutions in XRCC1 BRCC2 domain is Arg560Trp. Molecular mechanic (MM) and Monte Carlo (MC) was used for investigation biophysical chemistry properties for any type of XRCC1 BRCC2 domain (wild type or mutant) in any temperatures (290,292,294,296,298,300,302,304,306,308,309,310,311,312,313,314, and 315 K), and any mediums (vacuum or water).Assessments of potential energy (Kcal/mol) and Quantitative structure– activity relationship (QSAR) of XRCC1 BRCC2 domain revealed that polymorphism (Arg560Trp) is caused it become unstable. Therefore mutant type (Trp560) of this protein cannot interact with Lig3 as well as wild type (Arg560) and then DNA repair  is defected.

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Molecular mechanic and monte carlo study of polymorphism effects on biophysical chemistry properties of XRCC1 BRCT2 domain

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