Hydration of Intrinsically Disordered Proteins from Wide-Line NMR

Research output: Chapter in Book/Report/Conference proceedingChapter

6 Citations (Scopus)


The principal aim of our work is to characterize structural and dynamical properties of interfacial water at the protein surface by wide - line NMR spectroscopy and nuclear relaxation time measurements for the identification and characterization of intrinsically disordered proteins (IDPs) and to make a distinction between IDPs and globular proteins. Our approach is to explore the structure ? interface relations of IDPs and globular proteins. In this chapter, we provide a detailed description of the theoretical background and practice of this approach, followed by the description of its implementation on two proteins, the IDP early responsive to dehydration 10 (ERD10), and globular bovine serum albumin (BSA). The main results are the direct determination of the number of hydration water molecules, the elements of hydration water dynamics (activation energy and correlation times), and the differences in dynamics as seen by the different time windows provided by the different types of relaxation rates ( R 1 , R 1 ? and R 2 ). We show by these two examples that IDPs are distinguished from globular proteins by their more extended interfacial region (hydration), their stronger.

Original languageEnglish
Title of host publicationInstrumental Analysis of Intrinsically Disordered Proteins
Subtitle of host publicationAssessing Structure and Conformation
PublisherJohn Wiley and Sons
Number of pages24
ISBN (Print)9780470343418
Publication statusPublished - Sep 9 2010


  • Hydration of intrinsically disordered proteins - from wide-line NMR
  • NMR intensity versus temperature curves - for ERD10, BSA and buffer solutions
  • Nuclear relaxation rates - using density matrix formalism or conventional perturbation theory

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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    Tompa, K., Bokor, M., & Tompa, P. (2010). Hydration of Intrinsically Disordered Proteins from Wide-Line NMR. In Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation (pp. 345-368). John Wiley and Sons. https://doi.org/10.1002/9780470602614.ch12