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Why Inverse Proteins Are Relatively Abundant

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Abstract:

Studies have shown that inverse proteins are relatively abundant. In this work, we investigate the proposition that the repeat patterns they share with protein sequences explain this phenomenon. Using a new artificial set of peptide sequences which also display these features and a random set, we show that the presence of repeats contributes to protein sequence similarity. Further analysis confirms that most inverse proteins exhibit repeats. Therefore, we suggest the relative abundance of inverse proteins can be explained by the fact they display the same repeat structures and amino acid propensity of existing proteins.





Keywords: Amino acid propensity; inverse proteins; nullomers; random peptide chains; repeats

Document Type: Research Article

DOI: https://doi.org/10.2174/092986610791306698

Publication date: 2010-07-01

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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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