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Comment
. 2013 Feb 5;104(3):517-9.
doi: 10.1016/j.bpj.2012.12.029.

New and notable: key new insights into membrane targeting by proteins

Gregory A Voth  1
Affiliations
Comment

New and notable: key new insights into membrane targeting by proteins

Gregory A Voth. Biophys J. .
No abstract available

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Figures

Figure 1
Figure 1
MD results by Cui et al. (9) of N-BAR H0 helix binding and folding into curved membranes. (a) Typical configuration of the H0 for a flat or slightly bent region of the membrane. (Red dots) ASA packing defects. Hydrophobic insertions into these defects are seen for the H0 helix. (Bottom) Color-coded free energy surface for the H0 on the membrane surface as a function of two variables that describe its conformations, including the helical state as one limit (upper-right region) and the unstructured state (lower-left region). (b) H0 helix folded into a large defect on the highly curved surface of the membrane. (Bottom) Free energy surface has a distinct minimum around the folded state of the H0, with a number of higher local free energy minima for more unstructured states of H0. The higher free energy states still have multiple insertions into the membrane defects by some of the H0 hydrophobic residues.
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References

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