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Studies of membrane proteins have revealed a
direct link between the lipid environment and the structure and
function of some of these proteins. Although some of these effects
involve specific chemical interactions between lipids and protein
residues, many can be understood in terms of protein-induced
perturbations to the membrane shape. The free-energy cost of such
perturbations can be estimated quantitatively, and measurements of
channel gating in model systems of membrane proteins with their lipid
partners are now confirming predictions of simple models.
The role of continuum mechanics can be used to gain insight on
the energetical cost of inserting membrane proteins inside a lipid
bilayer. If the activity of the protein necessitates a change of
conformation, the bilayer energy difference associated with the
different structures can affect the probability of this transition.
This phenomenon, which could be at the origin of protein inhibition
following the insertion of membrane-interacting molecules (Fig.1),
can also be used to quantify the sensitivity of particular proteins, such as ion channels, to
the bilayer properties.
The paper below gives a review of the current theoretical understanding of the
mechancial interaction between a protein and the surrounding lipids,
and gives clue on the impact of these interaction on the probability of
transition between different protein states, which ultimately control
protein activity.
Emerging roles for lipids in shaping membrane-protein function
(R. Phillips, T. Ursell, P. Wiggins and P. Sens, Nature 459 379-385 (2009))
reprint (pdf)
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Fig.2 Two classes of membrane deformation around a membrane channel
(Left - MscL; Right - MscS) |
