Literature DB >> 11943177

High free energy of lipid/protein interaction in biological membranes.

Heinrich Sandermann1.   

Abstract

The free energy of lipid/protein interaction in biological membranes is still unknown although extensive partitioning and modelling studies have revealed many partial energetic increments. Multiple site binding kinetics are now applied to four well-studied functional membrane proteins, and mean free energy values (+/-S.D.) of -4.23+/-0.49 kcal/mol for single lipid binding sites and of -89.7+/-35.4 kcal/mol for complete lipid substitution are obtained. These high free energy values point to an important bioenergetic role of lipid/protein interaction in membrane functions.

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Year:  2002        PMID: 11943177     DOI: 10.1016/s0014-5793(02)02400-6

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

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Journal:  Chem Rev       Date:  2017-02-17       Impact factor: 60.622

3.  Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor.

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  3 in total

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