Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 349546
Title Anchoring mechanisms of membrane-associated M13 major coat protein
Author(s) Stopar, D.; Spruijt, R.B.; Hemminga, M.A.
Source Chemistry and Physics of Lipids 141 (2006)1-2. - ISSN 0009-3084 - p. 83 - 93.
DOI https://doi.org/10.1016/j.chemphyslip.2006.02.023
Department(s) Biophysics
EPS-2
Publication type Refereed Article in a scientific journal
Publication year 2006
Keyword(s) water interface - lipid-bilayers - nmr-spectroscopy - transmembrane domain - tryptophan residues - backbone dynamics - aromatic residues - bacteriophage m13 - solid-state - model
Abstract Bacteriophage M13 major coat protein is extensively used as a biophysical, biochemical, and molecular biology reference system for studying membrane proteins. The protein has several elements that control its position and orientation in a lipid bilayer. The N-terminus is dominated by the presence of negatively charged amino acid residues (Glu2, Asp4, and Asp5), which will always try to extend into the aqueous phase and therefore act as a hydrophilic anchor. The amphipathic and the hydrophobic transmembrane part contain the most important hydrophobic anchoring elements. In addition there are specific aromatic and charged amino acid residues in these domains (Phe 11, Tyr21, Tyr24, Trp26, Phe42, Phe45, Lys40, Lys43, and Lys44) that fine-tune the association of the protein to the lipid bilayer. The interfacial Tyr residues are important recognition elements for precise protein positioning, a function that cannot be performed optimally by residues with an aliphatic character. The Trp26 anchor is not very strong: depending on the context, the tryptophan residue may move in or out of the membrane. On the other hand, Lys residues and Phe residues at the C-terminus of the protein act in a unique concerted action to strongly anchor the protein in the lipid bilayer.
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