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- W2107799535 endingPage "15192" @default.
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- W2107799535 abstract "A question of fundamental importance concerning the biosynthesis of integral membrane proteins is whether transmembrane secondary structure can insert spontaneously into a lipid bilayer. It has proven to be difficult to address this issue experimentally because of the poor solubility in aqueous solution of peptides and proteins containing these extremely hydrophobic sequences. We have identified a system in which the kinetics and thermodynamics of α-helix insertion into lipid bilayers can be studied systematically and quantitatively using simple spectroscopic assays. Specifically, we have discovered that a 36-residue polypeptide containing the sequence of the C-helix of the integral membrane protein bacteriorhodopsin exhibits significant solubility in aqueous buffers free of both detergents and denaturants. This helix contains two aspartic acid residues in the membrane-spanning region. At neutral pH, the peptide associates with lipid bilayers in a nonhelical and presumably peripheral conformation. With a pKa of 6.0, the peptide inserts into the bilayer as a transbilayer α-helix. The insertion reaction proceeds rapidly at room temperature and is fully reversible." @default.
- W2107799535 created "2016-06-24" @default.
- W2107799535 creator A5002753770 @default.
- W2107799535 creator A5041462222 @default.
- W2107799535 creator A5042428472 @default.
- W2107799535 creator A5081230059 @default.
- W2107799535 date "1997-12-01" @default.
- W2107799535 modified "2023-10-11" @default.
- W2107799535 title "Spontaneous, pH-Dependent Membrane Insertion of a Transbilayer α-Helix" @default.
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