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  perfectBASH: Band-selective homonuclear decoupling in peptides and peptidomimetics.

Ilgen, J., Kaltschnee, L., & Thiele, C. M. (2018). perfectBASH: Band-selective homonuclear decoupling in peptides and peptidomimetics. Magnetic Resonance in Chemistry, 56(10), 918-933. doi:10.1002/mrc.4757.

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 Creators:
Ilgen, J., Author
Kaltschnee, L.1, Author           
Thiele, C. M., Author
Affiliations:
1Research Group of NMR Signal Enhancement, MPI for Biophysical Chemistry, Max Planck Society, ou_2396691              

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Free keywords: H-1-NMR; 2D NMR; band-selective homonuclear (BASH) decoupling; full sensitivity; NMR; peptides; peptidomimetics; perfect echo; pure shift
 Abstract: Pure shift techniques have recently attracted much attention, as they have the ability to reduce spectral overlap and thus to simplify the analysis of complex and congested spectral regions. For peptides, band-selective pure shift approaches are often the most reasonable choice among these, when spectra need to be simplified along proton dimensions. Band-selective approaches usually offer the highest sensitivity of all pure shift methods, albeit at the cost that signals can only be acquired in a single-frequency region of the spectrum, in which protons are well isolated in the proton spectrum. For -peptides, signals are usually acquired either in the amide-proton region or in the -proton region. Herein, we present experiments, which enable the pure shift acquisition in both the amide-proton and the -proton regions of -peptides simultaneously, without sacrificing the characteristics of band-selective pure shift methods to provide high sensitivity. The perfectBASH approach discussed here combines the perfect echo experiment with band-selective decoupling. It can be used for band-selective pure shift acquisition of H-1, TOCSY, CLIP-COSY, relayed CLIP-COSY, NOESY, and EASY-ROESY spectra, with proton-proton decoupling over the full backbone region of -peptides, which is most interesting for samples prepared without isotopic enrichment. As the utility of this technique is by no means limited to -peptides, we further illustrate its utility for H-1-NMR studies of a peptidomimetic oligourea.

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Language(s): eng - English
 Dates: 2018-06-082018-10
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/mrc.4757
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Title: Magnetic Resonance in Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 56 (10) Sequence Number: - Start / End Page: 918 - 933 Identifier: -