Rapid estimation of relative amide proton exchange rates of 15N‐labelled proteins by a straightforward water selective NOESY‐HSQC experiment

A straightforward heteronuclear pseudo‐3D NOESY‐HSQC pulse sequence using radiation damping to selectively invert magnetization at the water frequency was developed to estimate the amide proton exchange rates in 15N‐labelled proteins. The peak intensities in the resultant 2D spectrum allow a direct classification of amide proton exchange rates according to short (ms), intermediate (ms to s) or long (≥ s) residence times. This method was successfully used for the analysis of amide proton exchange rates in the 15N‐labelled FruR DNA‐binding domain and pertinent information about its dynamics was obtained.

• Publication year

  1996

• Venue

  FEBS Letters

• Publication date

  1996-04-01

• Fields of study

  Medicine, Chemistry

• Identifiers
  DOI 10.1016/0014-5793(96)00243-8PMID 8925894
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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