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Title: NMR studies on the surface accessibility of the archaeal protein Sso7d by using TEMPOL and Gd(III)(DTPA-BMA) as paramagnetic probes
Authors: Bernini, Andrea 
V., Venditti
Spiga, Ottavia 
A., Ciutti
F., Prischi
R., Consonni
L., Zetta
I., Arosio
P., Fusi
A., Guagliardi
Niccolai, Neri 
Keywords: Surface accessibility; Protein NMR; Paramagnetic probes; TEMPOL; Gd(III)(DTPA-BMA)
Issue Date: 2008
Project: None 
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 H-1-N-15 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). (C) 2008 Elsevier B.V. All rights reserved.
ISSN: 0301-4622
DOI: 10.1016/j.bpc.2008.07.003
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