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Target Peptide Recognition by S100P Protein and Role of Central Linker Region and Dimer Interface

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Interaction between S100P and its target protein is an essential step in several cellular functions. The amphiphatic mellitin peptide binds tightly to S100P protein in the presence of calcium cation. Since little is known about the recognition sequence, mellitin interaction form a model for S100P. Interaction between mellitin and protein examined to identify key regions required for the protein-protein interaction.

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Keywords: S100P; conformational change; peptide binding

Document Type: Research Article

Affiliations: Cumhuriyet Universitesi Kimya Bolumu Biyokimya A.B.D. Sivas Turkey 58140; Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409- 1061, USA.

Publication date: 2006-03-01

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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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