Residue-specific membrane location of peptides and proteins using specifically and extensively deuterated lipids and ¹³C-²H rotational-echo double-resonance solid-state NMR.
Residue-specific membrane location of peptides and proteins using specifically and extensively deuterated lipids and ¹³C-²H rotational-echo double-resonance solid-state NMR.
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DOI:
10.1007/s10858-012-9692-8
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发表时间:
2013-01
影响因子:
2.7
通讯作者:
Weliky DP
中科院分区:
文献类型:
--
作者:
Xie L;Ghosh U;Schmick SD;Weliky DP
Residue-specific location of peptides in the hydrophobic core of membranes was examined using 13C-2H REDOR and samples in which the lipids were selectively deuterated. The transmembrane topology of the KALP peptide was validated with this approach with substantial dephasing observed for deuteration in the bilayer center and reduced or no dephasing for deuteration closer to the headgroups. Insertion of β sheet HIV and helical and β sheet influenza virus fusion peptides into the hydrophobic core of the membrane was validated in samples with extensively deuterated lipids.
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