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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, A and Venditti, V and Spiga, O and Ciutti, A and Prischi, F and Consonni, R and Zetta, L and Arosio, I and Fusi, P and Guagliardi, A and Niccolai, N (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). 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
Subjects: Q Science > Q Science (General)
Divisions: Faculty of Science and Health > Biological Sciences, School of
Depositing User: Filippo Prischi
Date Deposited: 04 Feb 2016 11:50
Last Modified: 06 Feb 2019 06:15
URI: http://repository.essex.ac.uk/id/eprint/14833

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