MAS NMR detection of hydrogen bonds for protein secondary structure characterization.
 

MAS NMR detection of hydrogen bonds for protein secondary structure characterization.

Related Articles MAS NMR detection of hydrogen bonds for protein secondary structure characterization.

J Biomol NMR. 2020 Mar 17;:

Authors: Friedrich D, Perodeau J, Nieuwkoop AJ, Oschkinat H

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 ?-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 ?-sheet topologies and ?-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.


PMID: 32185644 [PubMed - as supplied by publisher]



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