Molecular Dynamics Study of Human MTHFR Wild-Type and A222V Mutant-Type: A Computational Approach

Methylenetetrahydrofolate reductase (MTHFR) is an essential enzyme for the homeostasis and metabolism of intracellular folate. However, it known that one commonly found MTHFR gene SNPs (A222V) causes a decrease in activity which decreases folate levels increases accumulation homocysteine blood. The purpose this study was to investigate molecular dynamics wild-type protein A222V mutant silico. After some preparations, crystal structure with code 6FCX obtained from Protein Data Bank used as input file (MD) simulations. YASARA-Structure employed performing 50 ns production run MD deviation root-mean-squared value backbone atoms (∆RMSDBb) consistently less than 2 Å beginning simulations runs. On other hand, there sudden spike ∆RMSDBb 15.01 20.00 2.221 Å. According analysis ∆RMSDBb, considered stable unstable may lead various clinical problems person possessing mutation.