The Experts below are selected from a list of 1011 Experts worldwide ranked by ideXlab platform
Ian R. Booth - One of the best experts on this subject based on the ideXlab platform.
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Properties of the Mechanosensitive Channel MscS Pore Revealed by Tryptophan Scanning Mutagenesis
2016Co-Authors: Tim Rasmussen, Akiko Rasmussen, Shivani Singh, Heloisa Galbiati, Michelle D. Edwards, Samantha Miller, Ian R. BoothAbstract:ABSTRACT: Bacterial mechanosensitive channels gate when the transmembrane turgor rises to levels that compromise the structural integrity of the cell wall. Gating creates a transient large diameter pore that allows hydrated Solutes to pass from the cytoplasm at rates close to those of diffusion. In the closed conformation, the channel limits transmembrane Solute Move-ment, even that of protons. In the MscS crystal structure (Protein Data Bank entry 2oau), a narrow, hydrophobic opening is visible in the crystal structure, and it has been proposed that a vapor lock created by the hydrophobic seals, L105 and L109, is the barrier to water and ions. Tryptophan scanning mutagenesis has proven to be a highly valuable tool for the analysis of channel structure. Here Trp residues were introduced along the pore-forming TM3a helix and in selected other parts of the protein. Mutants were investigated for their expression, stability, and activity and as fluorescent probes of the physical properties along th
Tim Rasmussen - One of the best experts on this subject based on the ideXlab platform.
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Properties of the Mechanosensitive Channel MscS Pore Revealed by Tryptophan Scanning Mutagenesis
2016Co-Authors: Tim Rasmussen, Akiko Rasmussen, Shivani Singh, Heloisa Galbiati, Michelle D. Edwards, Samantha Miller, Ian R. BoothAbstract:ABSTRACT: Bacterial mechanosensitive channels gate when the transmembrane turgor rises to levels that compromise the structural integrity of the cell wall. Gating creates a transient large diameter pore that allows hydrated Solutes to pass from the cytoplasm at rates close to those of diffusion. In the closed conformation, the channel limits transmembrane Solute Move-ment, even that of protons. In the MscS crystal structure (Protein Data Bank entry 2oau), a narrow, hydrophobic opening is visible in the crystal structure, and it has been proposed that a vapor lock created by the hydrophobic seals, L105 and L109, is the barrier to water and ions. Tryptophan scanning mutagenesis has proven to be a highly valuable tool for the analysis of channel structure. Here Trp residues were introduced along the pore-forming TM3a helix and in selected other parts of the protein. Mutants were investigated for their expression, stability, and activity and as fluorescent probes of the physical properties along th
Akiko Rasmussen - One of the best experts on this subject based on the ideXlab platform.
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Properties of the Mechanosensitive Channel MscS Pore Revealed by Tryptophan Scanning Mutagenesis
2016Co-Authors: Tim Rasmussen, Akiko Rasmussen, Shivani Singh, Heloisa Galbiati, Michelle D. Edwards, Samantha Miller, Ian R. BoothAbstract:ABSTRACT: Bacterial mechanosensitive channels gate when the transmembrane turgor rises to levels that compromise the structural integrity of the cell wall. Gating creates a transient large diameter pore that allows hydrated Solutes to pass from the cytoplasm at rates close to those of diffusion. In the closed conformation, the channel limits transmembrane Solute Move-ment, even that of protons. In the MscS crystal structure (Protein Data Bank entry 2oau), a narrow, hydrophobic opening is visible in the crystal structure, and it has been proposed that a vapor lock created by the hydrophobic seals, L105 and L109, is the barrier to water and ions. Tryptophan scanning mutagenesis has proven to be a highly valuable tool for the analysis of channel structure. Here Trp residues were introduced along the pore-forming TM3a helix and in selected other parts of the protein. Mutants were investigated for their expression, stability, and activity and as fluorescent probes of the physical properties along th
Shivani Singh - One of the best experts on this subject based on the ideXlab platform.
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Properties of the Mechanosensitive Channel MscS Pore Revealed by Tryptophan Scanning Mutagenesis
2016Co-Authors: Tim Rasmussen, Akiko Rasmussen, Shivani Singh, Heloisa Galbiati, Michelle D. Edwards, Samantha Miller, Ian R. BoothAbstract:ABSTRACT: Bacterial mechanosensitive channels gate when the transmembrane turgor rises to levels that compromise the structural integrity of the cell wall. Gating creates a transient large diameter pore that allows hydrated Solutes to pass from the cytoplasm at rates close to those of diffusion. In the closed conformation, the channel limits transmembrane Solute Move-ment, even that of protons. In the MscS crystal structure (Protein Data Bank entry 2oau), a narrow, hydrophobic opening is visible in the crystal structure, and it has been proposed that a vapor lock created by the hydrophobic seals, L105 and L109, is the barrier to water and ions. Tryptophan scanning mutagenesis has proven to be a highly valuable tool for the analysis of channel structure. Here Trp residues were introduced along the pore-forming TM3a helix and in selected other parts of the protein. Mutants were investigated for their expression, stability, and activity and as fluorescent probes of the physical properties along th
Heloisa Galbiati - One of the best experts on this subject based on the ideXlab platform.
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Properties of the Mechanosensitive Channel MscS Pore Revealed by Tryptophan Scanning Mutagenesis
2016Co-Authors: Tim Rasmussen, Akiko Rasmussen, Shivani Singh, Heloisa Galbiati, Michelle D. Edwards, Samantha Miller, Ian R. BoothAbstract:ABSTRACT: Bacterial mechanosensitive channels gate when the transmembrane turgor rises to levels that compromise the structural integrity of the cell wall. Gating creates a transient large diameter pore that allows hydrated Solutes to pass from the cytoplasm at rates close to those of diffusion. In the closed conformation, the channel limits transmembrane Solute Move-ment, even that of protons. In the MscS crystal structure (Protein Data Bank entry 2oau), a narrow, hydrophobic opening is visible in the crystal structure, and it has been proposed that a vapor lock created by the hydrophobic seals, L105 and L109, is the barrier to water and ions. Tryptophan scanning mutagenesis has proven to be a highly valuable tool for the analysis of channel structure. Here Trp residues were introduced along the pore-forming TM3a helix and in selected other parts of the protein. Mutants were investigated for their expression, stability, and activity and as fluorescent probes of the physical properties along th