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Structure and Function of Bovine Pancreatic Deoxyribonuclease I

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Bovine pancreatic deoxyribonuclease I (bpDNase), the first DNase discovered, is the best characterized among various types of DNase. A catalytic mechanism has been suggested based on the X-ray structure of the bpDNase-octamer complex. In this review, we will focus on three aspects: 1) the distinctive functions of the two structural calcium atoms; 2) the biological functions of the two disulfides; and 3) the involvement of the N- and C-terminal fragments in the enzyme folding for activity.

Keywords: Deoxyribonuclease; calcium; chemical modification; disulfide; enzyme mechanism; protein folding; site-directed mutagenesis

Document Type: Research Article


Affiliations: Institute of Biotechnology, College of Bioresources, National Ilan University and Institute of Biochemistry and Molecular Biology, College of Medicine, National Taiwan University, 1 Shen-Lung Rd. Sec. 1, Ilan 260, Taiwan.

Publication date: May 1, 2006

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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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