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• W2010517110 startingPage "1273" @default.
• W2010517110 abstract "Maltoporin allows permeation of long maltodextrin chains. It tightly binds the amphiphilic sugar, offering both hydrophobic interactions with a helical lane of aromatic residues and H bonds with ionic side chains. The minimum-energy path of maltohexaose translocation is obtained by the conjugate peak refinement method, which optimizes a continuous string of conformers without applying constraints. This reveals that the protein is passive while the sugar glides screw-like along the aromatic lane. Near instant switching of sugar hydroxyl H bond partners results in two small energy barriers (of approximately 4 kcal/mol each) during register shift by one glucosyl unit, in agreement with a kinetic analysis of experimental dissociation rates for varying sugar chain lengths. Thus, maltoporin functions like an efficient translocation enzyme, and the slow rate of the register shift (approximately 1/ms) is due to high collisional friction." @default.
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• W2010517110 date "2002-09-01" @default.
• W2010517110 modified "2023-10-13" @default.
• W2010517110 title "Translocation Mechanism of Long Sugar Chains across the Maltoporin Membrane Channel" @default.
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• W2010517110 doi "https://doi.org/10.1016/s0969-2126(02)00811-0" @default.
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