Abstract
The folding of alpha-helical membrane proteins has previously been described using the two stage model, in which the membrane insertion of independently stable alpha-helices is followed by their mutual interactions within the membrane to give higher order folding and oligomerization. Given recent advances in our understanding of membrane protein structure it has become apparent that in some cases the model may not fully represent the folding process. Here we present a three stage model which gives considerations to ligand binding, folding of extramembranous loops, insertion of peripheral domains and the formation of quaternary structure.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Aquaporins / chemistry
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Bacterial Proteins / chemistry
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Bacteriorhodopsins / chemistry
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Binding Sites
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Escherichia coli Proteins / chemistry
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Ligands
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Lipid Bilayers / chemistry
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Membrane Proteins / chemistry*
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Models, Molecular
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Potassium Channels / chemistry
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Protein Folding
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Protein Structure, Quaternary
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Thermodynamics
Substances
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Aquaporins
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Bacterial Proteins
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Escherichia coli Proteins
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Ligands
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Lipid Bilayers
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Membrane Proteins
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Potassium Channels
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prokaryotic potassium channel
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GlpF protein, E coli
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Bacteriorhodopsins