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Role of Cation-π Interactions in the Structural Stability of Bacterial Adhesins

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Attachment to host cell surfaces is a crucial step in bacterial infections. This step is mediated by important virulence factors termed adhesins which are protein in nature. Non-covalent interactions play an important role in the structural stability of protein molecules. In the present study, the roles played by cation-π interactions in the adhesion proteins of Gram negative bacilli, Gram negative cocci and Gram positive cocci are systematically analyzed. There are significant differences in the pattern of interactions and environmental preferences like secondary structure, solvent accessibility, and stabilization centers for the amino acid residues which are involved in interactions. Among the cationic residues the role of Arg is significant in Gram negative group, while in the case of Gram positive cocci the contribution from Lys is found to be important. These results might be useful for understanding the stability patterns of adhesins in different groups of pathogenic bacteria.
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Keywords: Adhesins; cation-π interactions; secondary structure; stabilization centers

Document Type: Research Article

Publication date: June 1, 2013

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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