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Comment
. 2004 Mar 23;101(12):3995-6.
doi: 10.1073/pnas.0400671101. Epub 2004 Mar 15.

Membrane proteins: a new method enters the fold

James U Bowie  1
Affiliations
Comment

Membrane proteins: a new method enters the fold

James U Bowie. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Fig. 1.
Fig. 1.
Membrane protein unfolding. For helical proteins, shown on the left, tertiary structure can be lost within the membrane environment, leaving stable transmembrane helices. Thus, the insertion of helices and folding (helix packing) can be separated. For β-barrel proteins, secondary structure should not be independently stable in the membrane. Thus, folding and insertion are likely to be coupled. The free energy of this folding and insertion equilibrium has now been measured by Hong and Tamm (2). They were able to study the effects of bilayer properties on this equilibrium. A mismatch between the hydrophobic width of the protein (green region) and the bilayer can induce distortions in either the protein or the bilayer. Cone-shaped lipids (yellow head group) lead to increased packing pressure in the center of the bilayer and decreased packing pressure at the head groups, which can be alleviated by the insertion of an hourglass-shaped protein.
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References

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