MAS NMR detection of hydrogen bonds for protein secondary structure characterization View Full Text


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Article Info

DATE

2020-03-17

AUTHORS

Daniel Friedrich, Jacqueline Perodeau, Andrew J. Nieuwkoop, Hartmut Oschkinat

ABSTRACT

Hydrogen bonds are essential for protein structure and function, making experimental access to long-range interactions between amide protons and heteroatoms invaluable. Here we show that measuring distance restraints involving backbone hydrogen atoms and carbonyl- or α-carbons enables the identification of secondary structure elements based on hydrogen bonds, provides long-range contacts and validates spectral assignments. To this end, we apply specifically tailored, proton-detected 3D (H)NCOH and (H)NCAH experiments under fast magic angle spinning (MAS) conditions to microcrystalline samples of SH3 and GB1. We observe through-space, semi-quantitative correlations between protein backbone carbon atoms and multiple amide protons, enabling us to determine hydrogen bonding patterns and thus to identify β-sheet topologies and α-helices in proteins. Our approach shows the value of fast MAS and suggests new routes in probing both secondary structure and the role of functionally-relevant protons in all targets of solid-state MAS NMR. More... »

PAGES

247-256

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    http://scigraph.springernature.com/pub.10.1007/s10858-020-00307-z

    DOI

    http://dx.doi.org/10.1007/s10858-020-00307-z

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1125713549

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/32185644


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