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• W2090800972 abstract "Plant ns-LTPs display an original structure with four helices and a flexible C-terminus, maintained together by four disulphide bridges and delineating an elongated central hydrophobic cavity. In order to relate these structural features to the protein stability and plasticity, combined molecular mechanics and simulated annealing calculations were undertaken on a wheat ns-LTP mutant with Cys-Ala replacement and with the application of core inter-residue restraints up to 2 A, reducing the cross-section size of the hydrophobic cavity. Analysis of the energy-minimized structures shows that removal of the disulphide bridges results in structures with a lower total energy and a smaller cavity volume. A 1-ns MD simulation at 300K in water, underlines that, despite the absence of a well-packed hydrophobic core, the native structure is extremely stable at room temperature and the cavity is not hydrated. This confirms that the disulphide bridges are essential for the existence of the cavity, whereas its plasticity depends both on the hydrophobic chain lining the cavity and on the C-terminal flexibility. A high temperature (500K) MD simulation confirms the stability of the secondary structure elements and the flexibility of the loops and of the C-terminal segment. Two important structural transitions during this simulation are discussed and possible routes for the insertion and release of hydrophobic ligands are suggested." @default.
• W2090800972 created "2016-06-24" @default.
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• W2090800972 date "2003-08-01" @default.
• W2090800972 modified "2023-10-17" @default.
• W2090800972 title "Protein Stability and Plasticity of the Hydrophobic Cavity in Wheat ns-LTP" @default.
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• W2090800972 doi "https://doi.org/10.1080/07391102.2003.10506902" @default.
• W2090800972 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12854956" @default.
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