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- W1036750606 abstract "Publisher Summary This chapter discusses about the membrane protein insertion. Membranes separate two aqueous compartments by a thin, two-dimensional, lipid phase. For most amino acids, there is no obvious statistical preference for a particular position within transmembrane sequences. The main feature of a signal sequence is a hydrophobic stretch of uncharged, mainly apolar residues. To achieve a transmembrane configuration, the protein entering the membrane from one face has to translocate one of its two hydrophilic ends. In eukaryotes, there is an additional class of proteins composed of an N-terminal cytoplasmic domain anchored in the membrane by a very C-terminal signal sequence. The topogenic contribution of the hydrophobic sequence was also shown to be important for natural proteins. Another mechanism that might be relevant is the exit of transmembrane segments out of the translocon into the lipid environment. This chapter stresses that the main driving force of helix bundling is hydrophobic interaction, which requires the matching of helix surfaces. Recently, the assembly of the tetrameric KcsA potassium channel from individual single-spanning subunits was studied." @default.
- W1036750606 created "2016-06-24" @default.
- W1036750606 creator A5041011253 @default.
- W1036750606 creator A5061756250 @default.
- W1036750606 date "2002-01-01" @default.
- W1036750606 modified "2023-09-23" @default.
- W1036750606 title "Membrane Protein Insertion into Bacterial Membraanes and the Endoplasmic Reticulum" @default.
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