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  Pulse EPR measurements of intramolecular distances in a TOPP-labeled transmembrane peptide in lipids.

Halbmair, K., Wegner, J., Diederichsen, U., & Bennati, M. (2016). Pulse EPR measurements of intramolecular distances in a TOPP-labeled transmembrane peptide in lipids. Biophysical Journal, 111(11), 2345-2348. doi:10.1016/j.bpj.2016.10.022.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-B981-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-6559-3
Genre: Journal Article

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Halbmair, K.1, Author              
Wegner, J., Author
Diederichsen, U., Author
Bennati, M.1, Author              
Affiliations:
1Research Group of Electron Paramagnetic Resonance, MPI for Biophysical Chemistry, Max Planck Society, ou_578606              

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 Abstract: We present the performance of nanometer-range pulse electron paramagnetic resonance distance measurements (pulsed electron-electron double resonance/double electron-electron resonance, PELDOR/DEER) on a transmembrane WALP24 peptide labeled with the semirigid unnatural amino acid 4-(3,3,5,5-tetra-methyl-2,6-dioxo-4-oxylpiperazin-1-yl)-l-phenylglycine (TOPP). Distances reported by the TOPP label are compared to the ones reported by the more standard MTSSL spin label, commonly employed in protein studies. Using high-power pulse electron paramagnetic resonance spectroscopy at Q-band frequencies (34 GHz), we show that in contrast to MTSSL, our label reports one-peak, sharp (Δr ≤ 0.4 nm) intramolecular distances. Orientational selectivity is not observed. When spin-labeled WALP24 was inserted in two representative lipid bilayers with different bilayer thickness, i.e., DMPC and POPC, the intramolecular distance reported by TOPP did not change with the bilayer environment. In contrast, the distance measured with MTSSL was strongly affected by the hydrophobic thickness of the lipid. The results demonstrate that the TOPP label is well suited to study the intrinsic structure of peptides immersed in lipids.

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Language(s): eng - English
 Dates: 2016-11-092016-12-06
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.bpj.2016.10.022
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Title: Biophysical Journal
Source Genre: Journal
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Pages: - Volume / Issue: 111 (11) Sequence Number: - Start / End Page: 2345 - 2348 Identifier: -