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
كليدواژه :
MD Simulation , AQP1 , SSNMR , NMR relaxation parameters (R1, R1⍴).
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.
