Interhelical hydrogen bonding drives strong interactions in membrane proteins

Polar residues in transmembrane α-helices may strongly influence the folding or association of integral membrane proteins. To test whether a motif that promotes helix association in a soluble protein could do the same within a membrane, we designed a model transmembrane helix based on the GCN4 leuci...

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Veröffentlicht in:	Nature Structural Biology 2000-02, Vol.7 (2), p.154-160
Hauptverfasser:	Xiao Zhou, Fang, Cocco, Melanie J., Russ, William P., Brunger, Axel T., Engelman, Donald M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Motifs Amino Acid Sequence Asparagine - chemistry Biochemistry Biological membranes Biological Microscopy Biomedical and Life Sciences Cell Membrane - metabolism Chloramphenicol O-Acetyltransferase - chemistry Chloramphenicol O-Acetyltransferase - genetics Chloramphenicol O-Acetyltransferase - metabolism Circular Dichroism Detergents - chemistry Dimerization DNA-Binding Proteins Electrophoresis, Polyacrylamide Gel Fungal Proteins - chemistry Glycophorin - chemistry Glycophorin - genetics Glycophorin - metabolism Hydrogen Hydrogen Bonding Leucine Zippers Life Sciences Magnetic Resonance Spectroscopy Membrane Biology Membrane Proteins - chemistry Membrane Proteins - metabolism Micelles Micrococcal Nuclease - chemistry Molecular Sequence Data Peptides - chemistry Protein Conformation Protein Kinases - chemistry Protein Structure Protein Structure, Secondary Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Saccharomyces cerevisiae Proteins
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