Detection of a transient intramolecular hydrogen bond using (l)J(NH) scalar 
couplings.

Xiang, S. Q.; Zweckstetter, M.

doi:10.1016/j.jmr.2014.04.004

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Detection of a transient intramolecular hydrogen bond using (l)J(NH) scalar couplings.

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Xiang, S. Q.
Research Group of Solid-State NMR, MPI for Biophysical Chemistry, Max Planck Society;

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Zweckstetter, M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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http://www.sciencedirect.com/science/article/pii/S1090780714001104/pdfft?md5=316247b1174e0246b002b494e9890c45&pid=1-s2.0-S1090780714001104-main.pdf
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Citation

Xiang, S. Q., & Zweckstetter, M. (2014). Detection of a transient intramolecular hydrogen bond using (l)J(NH) scalar couplings. Journal of Magnetic Resonance, 243, 93-97. doi:10.1016/j.jmr.2014.04.004.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-DBD2-4

Abstract

Hydrogen bonds are essential for the structure, stability and folding of proteins. The identification of intramolecular hydrogen bonds, however, is challenging, in particular in transiently folded states. Here we studied the presence of intramolecular hydrogen bonds in the folding nucleus of the coiled-coil structure of the GCN4 leucine zipper. Using one-bond (l)JNH spin spin coupling constants and hydrogen/deuterium exchange, we demonstrate that a transient intramolecular hydrogen bond is present in the partially helical folding nucleus of GCN(16-31). The data demonstrate that lJNH couplings are a sensitive tool for the detection of transient intramolecular hydrogen bonds in challenging systems where the effective/useable protein concentration is low. This includes peptides at natural abundance but also uniformly labeled biomolecules that are limited to low concentrations because of precipitation or aggregation.