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Open Access Highly Accessed Research article

Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface

Alessandro Siglioccolo, Alessandro Paiardini, Maria Piscitelli and Stefano Pascarella*

Author Affiliations

Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Università di Roma La Sapienza, 00185 Roma, Italy

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BMC Structural Biology 2011, 11:50  doi:10.1186/1472-6807-11-50

Published: 22 December 2011

Additional files

Additional file 1:

Table S1 - ΔASA in the SALTIN and OSMOL samples at conserved residues. Differences of fractional accessibility surface area (ΔASA) in the SALTIN and OSMOL samples for different class of atoms. The differences are between the surface areas calculated in the halophilic protein and the corresponding areas in the non-halophilic counterpart. The calculations were performed considering the proteins in their quaternary structure. Only residues identically conserved in the two proteins were considered in the calculations.

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Additional file 2:

Additional Figure 1 - ΔΔApAU-F. Histograms reporting the ΔΔApAU-F in the SALTIN and OSMOL samples. The ΔΔApAU-F values were calculated as the difference between the fraction of exposed apolar area lost during folding of the halophilic protein and the fraction lost by the corresponding non-halophilic homolog. Further details are reported in the "Methods" section of the main text.

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Additional file 3:

Additional Figure 2 - Correlation between single ΔACA and pairwise percentage identity. Graph reporting the difference between the area of each halophilic CHC and that of the corresponding non-halophilic CHC (ΔACA) versus the pairwise sequence percentage identity (%id) for the SALTIN and OSMOL samples.

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