integral membrane protein

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integral membrane protein

[¦int·i·grəl ′mem‚brān ‚prō‚tēn]
(cell and molecular biology)
A protein that is firmly anchored in the plasma membrane via interactions between its hydrophobic domains and the membrane phospholipids. Also known as intrinsic protein.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
References in periodicals archive ?
In these lipids domains, cholesterol increases the order of lipid-acyl chains, increasing the local membrane thickness and limiting the type of integral membrane proteins located on this hydrophobic environment.
Aquaporin is a kind of integral membrane proteins, which transport water molecules across membrane selectively and efficiently.
Pex3p, Pex16p, and Pex19p were identified as essential factors for assembly of peroxisomal integral membrane proteins (PMPs) in several species including humans (25), (47), (68), (69), (84)-(89) (Fig.
Caveolins are integral membrane proteins with molecular weight of 21 - 24 kDa, and as the scaffold structure, they recruit a lot of signal molecules.
Principles governing amino acid composition of integral membrane proteins: Applications to topology prediction.
integral membrane proteins, are thus specialized in detecting extra cellular signals and translating the information to the cell, allowing a response.
von Heijne, "Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms," Protein Science, vol.
In contrast to proteins which usually exist in one of two incompatible conformations associated with water-soluble and integral membrane proteins, PFTs show dimorphism in existing initially as water-soluble monomers and terminally as [beta]-barrel transmembrane oligomeric pores in the functionally active stage.
What they have to say about them includes native membrane protein versus yeast recombinant as demonstrated by the mitochondrial ADP/ATP carrier, the sarcoplasma calcium pump as an example of what can be learned about the function of a single protein from its various x-ray structures, two-dimensional crystallization of integral membrane proteins for electron crystallography, observing both secondary and tertiary structure in membrane protein fragments, and a critical review of general guidelines for membrane protein model building and analysis.
While the restriction with regard to these limitations mentioned above is usually compensated for by particular biochemical techniques, mainly liquid chromatography tandem mass spectrometry (LC-MS/MS), exploiting LC-MS/MS for comparative investigations of integral membrane proteins are currently raised (Wu and Yates, 2003).
to offer the first system for rapidly and reproducibly characterizing the binding affinities of antibodies to diverse integral membrane proteins, including GPCRs and ion channels.