NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins

M. Bokor, Veronika Csizmók, Dénes Kovács, P. Bánki, P. Friedrich, Peter Tompa, K. Tompa

Research output: Contribution to journalArticle

63 Citations (Scopus)

Abstract

Intrinsically unstructured/disordered proteins (IUPs) exist in a disordered and largely solvent-exposed, still functional, structural state under physiological conditions. As their function is often directly linked with structural disorder, understanding their structure-function relationship in detail is a great challenge to structural biology. In particular, their hydration and residual structure, both closely linked with their mechanism of action, require close attention. Here we demonstrate that the hydration of IUPs can be adequately approached by a technique so far unexplored with respect to IUPs, solid-state NMR relaxation measurements. This technique provides quantitative information on various features of hydrate water bound to these proteins. By freezing nonhydrate (bulk) water out, we have been able to measure free induction decays pertaining to protons of bound water from which the amount of hydrate water, its activation energy, and correlation times could be calculated. Thus, for three IUPs, the first inhibitory domain of calpastatin, microtubule-associated protein 2c, and plant dehydrin early responsive to dehydration 10, we demonstrate that they bind a significantly larger amount of water than globular proteins, whereas their suboptimal hydration and relaxation parameters are correlated with their differing modes of function. The theoretical treatment and experimental approach presented in this article may have general utility in characterizing proteins that belong to this novel structural class.

Original languageEnglish
Pages (from-to)2030-2037
Number of pages8
JournalBiophysical Journal
Volume88
Issue number3
DOIs
Publication statusPublished - Mar 2005

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Intrinsically Disordered Proteins
Water
Proteins
Microtubule-Associated Proteins
Dehydration
Freezing
Protons

ASJC Scopus subject areas

  • Biophysics

Cite this

NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins. / Bokor, M.; Csizmók, Veronika; Kovács, Dénes; Bánki, P.; Friedrich, P.; Tompa, Peter; Tompa, K.

In: Biophysical Journal, Vol. 88, No. 3, 03.2005, p. 2030-2037.

Research output: Contribution to journalArticle

Bokor, M. ; Csizmók, Veronika ; Kovács, Dénes ; Bánki, P. ; Friedrich, P. ; Tompa, Peter ; Tompa, K. / NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins. In: Biophysical Journal. 2005 ; Vol. 88, No. 3. pp. 2030-2037.
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