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Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation

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  • Mengjun Xue
  • ,
  • Ryo Kitahara, College of Pharmaceutical Sciences, Ritsumeikan University, Shiga 525-8577, Japan
  • ,
  • Yuichi Yoshimura
  • ,
  • Frans A A Mulder

Hydrogen exchange (HX) NMR spectroscopy is widely used for monitoring structure, stability and dynamics of proteins at the level of individual residues. The stochastic replacement of protons by deuterons typically leads to an exponential decrease of the NMR signals. However, an unusual signal increase was observed in HX of several amides for T4 lysozyme L99A. This effect can be attributed to peak sharpening as a result of reduced dipolar relaxation from proximal amide protons that experience more rapid hydrogen/deuterium (H/D) exchange. The behavior was specifically observed at the termini of secondary structure elements, where large differences in protection against H/D exchange are observed. This effect is expected to be more widespread in NMR HX studies, and is important for the accurate determination of protection factors.

Original languageEnglish
JournalBiochemical and Biophysical Research Communications
Pages (from-to)1185-1188
Number of pages4
Publication statusPublished - 2016

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