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Frequencies of Specific Peptides in Intrinsic Disordered Protein Domains

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We evaluated the i-peptides occurrence frequency in the protein sequences, belonging to two reference datasets containing structured and disordered protein domains. Moreover we estimated the most frequent i-peptides (with i= 2, 3, 4) into these sequences in order to select specific i-peptides for each structural classification. According to these specific ipeptides, a new binary classification method was developed for predicting if a given protein sequence can be classified as “disordered” or “structured”. The best results were obtained using the tri-peptides, much more able to gain structural information from sequences compared to the di-peptides.

Keywords: (AC); (IUPs); (NACP); 25PDB; 3-Dstructure; AD; Binary classification method; CASP8; CGI; CH-plot; DNA; DisProt; PREC-LASSPRO; PREDISPRO; correlation coefficient; disorder; disorder prediction; disordered; disordered proteins; hydrophilic; i-peptides; method; p53; peptides; peptides occurrence frequency; protein; protein folding; protein unfolding; specific i-peptides; unfolding; validation; weighted score

Document Type: Research Article

Publication date: 2010-11-01

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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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