The kamikaze approach to membrane transport.

H R Kaback, M Sahin-Tóth, A B Weinglass

Journal: Nature reviews. Molecular cell biology 2001;2(8):610-20

PMID: 11483994

Full Text on Nature Publishing Group View on PubMed

Abstract

Membrane transport proteins catalyse the movement of molecules into and out of cells and organelles, but their hydrophobic and metastable nature often makes them difficult to study by traditional means. Novel approaches that have been developed and applied to one membrane transport protein, the lactose permease from Escherichia coli, are now being used to study various other membrane proteins.

Address: Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles, California 90095-1662, USA. [email protected]

DOI: 10.1038/35085077

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MeSH Terms: Alkylation, Amino Acid Sequence, Bacterial Proteins, Binding Sites, Biological Transport, Carrier Proteins, Cysteine, Escherichia coli, Escherichia coli Proteins, Ethylmaleimide, Humans, Lactose, Long QT Syndrome, Membrane Proteins, Membrane Transport Proteins, Metabolism, Inborn Errors, Models, Molecular, Molecular Sequence Data, Monosaccharide Transport Proteins, Mutagenesis, Site-Directed, Protein Conformation, Protons, Recombinant Fusion Proteins, Structure-Activity Relationship, Sulfhydryl Reagents, Symporters