شماره ركورد كنفرانس
5328
عنوان مقاله
Monitoring Dynamics of Membrane protein in lipid bilayer environment by solid‐state NMR and Molecular Dynamics Simulations
پديدآورندگان
Razmazma Hafez Molecular Microbiology and Structural Biochemistry, University of Lyon, CNRS, UMR5086, Lyon, France , Ollila Samuli samuli.ollila@helsinki.fi b Institute of Biotechnology, University of Helsinki, Helsinki 00014, Finland , Ebrahimi Ali ebrahimi@chem.usb.ac.ir Department of Chemistry, University of Sistan and Baluchestan, Zahedan 98167-45845, Iran , Bonaccorsid Marta guido.pintacuda@ens-lyon.fr University of Lyon, Centre de RMN à Très hauts Champs, UMR 5280 CNRS, Villeurbanne, France , Pintacuda Guido University of Lyon, Centre de RMN à Très hauts Champs, UMR 5280 CNRS, Villeurbanne, France , Monticelli Luca luca.monticelli@ibcp.fr Molecular Microbiology and Structural Biochemistry, University of Lyon, CNRS, UMR5086, Lyon, France
تعداد صفحه
2
كليدواژه
MD Simulation , AQP1 , SSNMR , NMR relaxation parameters (R1, R1⍴).
سال انتشار
1400
عنوان كنفرانس
بيست و سومين كنفرانس شيمي فيزيك انجمن شيمي ايران
زبان مدرك
انگليسي
چكيده فارسي
In this work, we developed novel methodology to measure order parameters (S 2 ) 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.
كشور
ايران
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