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Post-translational modification of barley LTP1b: the lipid adduct lies in the hydrophobic cavity and alters the protein dynamics |
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| Authors: | Wijesinha-Bettoni Ramani Gao Chunli Jenkins John A Mackie Alan R Wilde Peter J Mills E N Clare Smith Lorna J |
| Institution: | Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford OX1 3QR, UK. |
| Abstract: | NMR techniques have been used to characterise the effects of a lipid-like post-translational modification on barley lipid transfer protein (LTP1b). NMR chemical shift data indicate that the lipid-like molecule lies in the hydrophobic cavity of LTP1b, with Tyr 79 being displaced to accommodate the ligand in the cavity. The modified protein has a reduced level of backbone amide hydrogen exchange protection, presumably reflecting increased dynamics in the protein. This may result from a loosening of the protein structure and may explain the enhanced surface properties observed for LTP1b. |
| Keywords: | COSY correlated spectroscopy DQF double quantum filtered LTP1 non-specific lipid transfer protein 1 LTP1b post-translationally modified LTP1 NOESY nuclear Overhauser enhancement spectroscopy TOCSY total correlation spectroscopy |
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