Protein Structure Prediction and Molecular Dynamics Simulation: Structure Prediction of Wild-Type Human MTHFR, Comparison with Mutants and MD Simulation of the Final Model - Brossura
Sinossi
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.
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Informazioni sugli autori
Khuram Shahzad: MS Bioinformatics,Department of Animal Sciences,UIUC,USA. Expertise:- Structural Bioinformatics and System Biology, Contact: khuramsb@gmail.com; Asifa Ahmed: Assistant Professor,CIIT,Islamabad,Pakistan,Exp:-Proteomics and Biochemistry; Zaheer ul Haq: Assistant Professor, PCMD,Karachi, Pakistan,Exp:-Computational Medicinal Chemistry.
Khuram Shahzad: MS Bioinformatics,Department of Animal Sciences,UIUC,USA. Expertise:- Structural Bioinformatics and System Biology, Contact: khuramsb@gmail.com; Asifa Ahmed: Assistant Professor,CIIT,Islamabad,Pakistan,Exp:-Proteomics and Biochemistry; Zaheer ul Haq: Assistant Professor, PCMD,Karachi, Pakistan,Exp:-Computational Medicinal Chemistry.
Khuram Shahzad: MS Bioinformatics,Department of Animal Sciences,UIUC,USA. Expertise:- Structural Bioinformatics and System Biology, Contact: khuramsb@gmail.com; Asifa Ahmed: Assistant Professor,CIIT,Islamabad,Pakistan,Exp:-Proteomics and Biochemistry; Zaheer ul Haq: Assistant Professor, PCMD,Karachi, Pakistan,Exp:-Computational Medicinal Chemistry.
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Protein Structure Prediction and Molecular Dynamics Simulation: Structure Prediction of Wild-Type Human MTHFR, Comparison with Mutants and MD Simulation of the Final Model
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Protein Structure Prediction and Molecular Dynamics Simulation | Structure Prediction of Wild-Type Human MTHFR, Comparison with Mutants and MD Simulation of the Final Model
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Taschenbuch. Condizione: Neu. Protein Structure Prediction and Molecular Dynamics Simulation | Structure Prediction of Wild-Type Human MTHFR, Comparison with Mutants and MD Simulation of the Final Model | Khuram Shahzad (u. a.) | Taschenbuch | Einband - flex.(Paperback) | Englisch | 2010 | VDM Verlag Dr. Müller | EAN 9783639300277 | Verantwortliche Person für die EU: OmniScriptum GmbH & Co. KG, Bahnhofstr. 28, 66111 Saarbrücken, info[at]akademikerverlag[dot]de | Anbieter: preigu. Codice articolo 107256818
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Protein Structure Prediction and Molecular Dynamics Simulation : Structure Prediction of Wild-Type Human MTHFR, Comparison with Mutants and MD Simulation of the Final Model
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Taschenbuch. Condizione: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - 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. Codice articolo 9783639300277
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