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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-DBD2-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-606F-E
Genre: Journal Article

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2039338.pdf (Publisher version), 901KB
 
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 Creators:
Xiang, S. Q.1, Author              
Zweckstetter, M.2, Author              
Affiliations:
1Research Group of Solid-State NMR, MPI for Biophysical Chemistry, Max Planck Society, ou_persistent35              
2Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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Free keywords: NMR spectroscopy; Scalar coupling; Hydrogen bond; Folding
 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.

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Language(s): eng - English
 Dates: 2014-04-182014-06
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.jmr.2014.04.004
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Title: Journal of Magnetic Resonance
Source Genre: Journal
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Pages: - Volume / Issue: 243 Sequence Number: - Start / End Page: 93 - 97 Identifier: -