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A BIOINFORMATICS STUDY OF THE SURFACE PROPERTIES OF HUMAN AND BACTERIAL ALDOLASES
Abstract:
This study reveals that human and bacterial class I and class II aldolases, despite their low sequence similarity, present similar global fractal characteristics of their surfaces. Their surface fractal dimensions correspond to those reported in specific literature for globular proteins. There is one exception, bacterial aldolase class I, which shows a higher surface roughness confirming the dissimilarity of its active sites in comparison to other investigated aldolases and also its distinct evolution. The electrical properties of surfaces for the investigated proteins show that class II of aldolases have higher dipole moments and quite larger contact potentials, explaining the presence of active sites for Zn2+, K+ and NH4+ ions.

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