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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Carrier Proteins / chemistry*
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Deuterium Exchange Measurement
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Fatty Acid-Binding Proteins
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Hordeum / chemistry*
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Hordeum / genetics
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Hordeum / metabolism*
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Hydrophobic and Hydrophilic Interactions*
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Lipid Metabolism
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Lipids / chemistry*
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Models, Molecular
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular
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Protein Processing, Post-Translational*
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Protein Structure, Tertiary
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Surface Properties
Substances
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Carrier Proteins
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Fatty Acid-Binding Proteins
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Lipids
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Ltp1 protein, barley