Dimerization and Ion Binding Properties of S100P Protein

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Abstract:

Functional S100P requires dimer formation and dimerization might form for one of the two reasons: i. producing a pair of site for target protein binding or ii. modulation of cation binding affinity. The extent of exposed protein hydrophobicity was related to dimer formation.





Keywords: Calcium; S100P; cation binding; dimer formation; prostate cancer

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986606775338425

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: March 1, 2006

More about this publication?
  • 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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