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Functional relevant dynamics study of fatty acid binding protein by NMR relaxation

Project: Functional relevant dynamics study of fatty acid binding protein by NMR relaxation

Source: National Natural Science Foundation of China

Type: Major International (Regional) Joint Research Program


Maili Liu  (Institute of Physics and Mathematics, CAS)


Daiwen Yang  (Department of Biological Sciences and Department of Chemistry, National University of Singapore)

Time: 2006-2008

Introduction: The project established and developed a number of NMR methods for protein dynamic analysis: NMR based detection of picosecond to nanosecond time scale dynamics of methyl and NMR based determination of microsecond to millisecond time scale dynamics of amide, and the methods have been applied to investigate the dynamics of fatty acid binding protein( FABP) in the absence and presence of fatty acids, in have been found that methyl groups from residues (M18, M21, V23, and A73) interact with the methyl group of the fatty acid become very rigid in the presence of fatty acids, and a number of methyl groups (V8, I90, I108, I109, and I127) that are far away from the binding sites also show increases in S2 when IFABP binds to a fatty acid. This may result from changes of side-chain orientations instead of mobility or from long-range conformational couplings to the residues in the binding regions.


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