期刊
NATURE COMMUNICATIONS
卷 5, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms5863
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资金
- NIH [RO1 GM74637, PO1 GM86685]
- Royal Society
- National Natural Science Foundation of China [BC4190004]
- Young 1,000 Talent
- Swedish Cancer Foundation
- Swedish Research Council
- Swedish Foundation for Strategic Research
- European Research Council [ERC-2008-AdG 232648]
- Knut and Alice Wallenberg Foundation
- UK BBSRC
- Marie Curie Senior Fellowship
- ISA
- ANKA
- BSRF (China)
- BBSRC [BB/J019135/1, BB/H023852/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/J019135/1, BB/H023852/1] Funding Source: researchfish
The favourable transfer free energy for a transmembrane (TM) alpha-helix between the aqueous phase and lipid bilayer underlies the stability of membrane proteins. However, the connection between the energetics and process of membrane protein assembly by the Sec61/SecY translocon complex in vivo is not clear. Here, we directly determine the partitioning free energies of a family of designed peptides using three independent approaches: an experimental microsomal Sec61 translocon assay, a biophysical (spectroscopic) characterization of peptide insertion into hydrated planar lipid bilayer arrays, and an unbiased atomic-detail equilibrium folding-partitioning molecular dynamics simulation. Remarkably, the measured free energies of insertion are quantitatively similar for all three approaches. The molecular dynamics simulations show that TM helix insertion involves equilibrium with the membrane interface, suggesting that the interface may play a role in translocon-guided insertion.
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