monitoring dynamics of membrane protein in lipid bilayer environment by solid‐state nmr and molecular dynamics simulations

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.