| Monitoring Dynamics of Membrane protein in lipid bilayer environment by solid‐state NMR and Molecular Dynamics Simulations |
| کد مقاله : 1195-PHYCHEM23 |
| نویسندگان |
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Hafez RAZMAZMA *1، Samuli Ollila2، Ali Ebrahimi3، Marta Bonaccorsi4، Guido Pintacuda4، Luca Monticelli5 1Molecular Microbiology and Structural Biochemistry, University of Lyon, CNRS, UMR5086, Lyon, France Department of Chemistry, University of Sistan and Baluchestan, Zahedan 98167-45845, Iran 2Institute of Biotechnology, University of Helsinki, Helsinki 00014, Finland 3Laboratory of Computational Quantum Chemistry and Drug Design, Department of Chemistry, University of Sistan and Baluchestan, Zahedan 98167-45845, Iran 4University of Lyon, Centre de RMN à Très hauts Champs, UMR 5280 CNRS, Villeurbanne, France 5Molecular Microbiology and Structural Biochemistry, University of Lyon, CNRS, UMR5086, Lyon, France |
| چکیده مقاله |
| In this work, we developed novel methodology to measure order parameters (S2) and spin relaxation rates (R1, R1⍴) of protein backbone and side chains in a lipid bilayer environment by solid state (SS) NMR spectroscopy; then we developed a protocol to calculate same NMR parameters from all-atom (AA) MD simulations. We applied the methodology to aquaporin 1 (AQP1), an important integral membrane protein. We find reasonable agreement between measured and calculated values. |
| کلیدواژه ها |
| MD Simulation; AQP1; SS-NMR; NMR relaxation parameters (R1, R1⍴). |
| وضعیت: پذیرفته شده برای ارسال فایل های ارائه پوستر |