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Updated: Jan 13, 2026

12:27
Measuring Peptide Translocation into Large Unilamellar Vesicles
Published on: January 27, 2012
14.2K
ペプチド特性は保護抗原ナノポアを介した多状態遷移速度論を予測する
Jennifer M Colby1, Bryan A Krantz2
1Molecular Toxicology Graduate Program, University of California, Berkeley, California.
Biophysical journal
|January 11, 2026
まとめ
炭疽菌毒素保護抗原(PA)ナノポアを介したペプチドの転送は、多状態メカニズムに従う。疎水性、立体、芳香族性が、ペプチドの移動と放出の特定のステップを決定する。
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Translocation of Proteins into the Mitochondria
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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Energy to Drive Translocation
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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
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