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NMR studies on the surface accessibility of the archaeal protein Sso7d by using TEMPOL and Gd(III)(DTPA-BMA) as paramagnetic probes

Bernini, Andrea and Venditti, Vincenzo and Spiga, Ottavia and Ciutti, Arianna and Prischi, Filippo and Consonni, Roberto and Zetta, Lucia and Arosio, Ivana and Fusi, Paola and Guagliardi, Annamaria and Niccolai, Neri (2008) 'NMR studies on the surface accessibility of the archaeal protein Sso7d by using TEMPOL and Gd(III)(DTPA-BMA) as paramagnetic probes.' Biophysical Chemistry, 137 (2-3). pp. 71-75. ISSN 0301-4622

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Abstract

Understanding how proteins are approached by surrounding molecules is fundamental to increase our knowledge of life at atomic resolution. Here, the surface accessibility of a multifunctional small protein, the archaeal protein Sso7d from Sulfolobus solfataricus, has been investigated by using TEMPOL and Gd(III)(DTPA-BMA) as paramagnetic probes. The DNA binding domain of Sso7d appears very accessible both to TEMPOL and Gd(III)(DTPA-BMA). Differences in paramagnetic attenuation profiles of 1H-15N HSQC protein backbone amide correlations, observed in the presence of the latter paramagnetic probes, are consistent with the hydrogen bond acceptor capability of the N-oxyl moiety of TEMPOL to surface exposed Sso7d amide groups. By using the gadolinium complex as a paramagnetic probe a better agreement between Sso7d structural features and attenuation profile is achieved. It is interesting to note that the protein P-loop region, in spite of the high surface exposure predicted by the available protein structures, is not approached by TEMPOL and only partially by Gd(III)(DTPA-BMA). © 2008 Elsevier B.V. All rights reserved.

Item Type: Article
Uncontrolled Keywords: Surface accessibility; Protein NMR; Paramagnetic probes; TEMPOL; Gd(III)(DTPA-BMA)
Subjects: Q Science > Q Science (General)
Divisions: Faculty of Science and Health
Faculty of Science and Health > Life Sciences, School of
SWORD Depositor: Elements
Depositing User: Elements
Date Deposited: 04 Feb 2016 11:50
Last Modified: 15 Jan 2022 00:30
URI: http://repository.essex.ac.uk/id/eprint/14833

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