Polar/Ionizable Residues in Transmembrane Segments: Effects on Helix-Helix Packing
Polar/Ionizable Residues in Transmembrane Segments: Effects on Helix-Helix Packing
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Publisher
United States: Public Library of Science
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Language
English
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Publisher
United States: Public Library of Science
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Scope and Contents
Contents
The vast majority of membrane proteins are anchored to biological membranes through hydrophobic α-helices. Sequence analysis of high-resolution membrane protein structures show that ionizable amino acid residues are present in transmembrane (TM) helices, often with a functional and/or structural role. Here, using as scaffold the hydrophobic TM doma...
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Full title
Polar/Ionizable Residues in Transmembrane Segments: Effects on Helix-Helix Packing
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TN_cdi_plos_journals_1326545269
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1326545269
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ISSN
1932-6203
E-ISSN
1932-6203
DOI
10.1371/journal.pone.0044263
