Andere Kunden interessierten sich auch für
![Monte Carlo Simulation Method for Protein Native Structure Prediction]( "Monte Carlo Simulation Method for Protein Native Structure Prediction")
Monte Carlo Simulation Method for Protein Native Structure Prediction45,99 €![Protein Structure Prediction]( "Protein Structure Prediction")
Protein Structure Prediction183,99 €![A Linear Regression Approach to Protein Secondary Structure Prediction]( "A Linear Regression Approach to Protein Secondary Structure Prediction")
A Linear Regression Approach to Protein Secondary Structure Prediction41,99 €![Molecular dynamics of mineral nanocrystal structures]( "Molecular dynamics of mineral nanocrystal structures")
Molecular dynamics of mineral nanocrystal structures29,99 €![Computational Modeling of Microtubule Structure and Assembly]( "Computational Modeling of Microtubule Structure and Assembly")
Computational Modeling of Microtubule Structure and Assembly38,99 €![Protein Structure Prediction]( "Protein Structure Prediction")
Protein Structure Prediction116,99 €![Understanding Protein Folding using Molecular Dynamics Simulation]( "Understanding Protein Folding using Molecular Dynamics Simulation")
Understanding Protein Folding using Molecular Dynamics Simulation53,99 €
Structure Prediction is one of the most important aspects of Structural Bioinformatics, Protein Docking and Drug Designing. The current study is performed on MTHFR enzyme. It plays an important role in folate and homocysteine metabolism by catalyzing the conversion of 5,10-methylenetetrahydrofolate to 5- methyltetrahydrofolate, used for homocysteine remethylation to methionine. MTHFR mutations have been found in a large number of diseases. However, the structure of MTHFR is still unknown, thereby limiting the understanding of structure function relationship to the diseased state. Different Bioinformatics methodologies were used to predict and compare the 3D structure of the wild-type and its mutants. The predicted models were visualized by VMD, RasMol and Pymol. Evaluation of the predicted models was performed using DFIRE, Verify3D, ANOLEA and PROCHECK. Selected Model was compared with its mutants and then simulated. MTHFR mutants were seen to have decreased number of serine phosphorylation sites as compared to wild-type. Phosphorylation seems to be playing a significant role in function of this enzyme.