Predictors of natively unfolded proteins: unanimous consensus score to detect a twilight zone between order and disorder in generic datasets |
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Authors: | Antonio Deiana Andrea Giansanti |
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Institution: | (1) Department of Physics, La Sapienza University of Rome, P.le A. Moro 5, 00185 Rome, Italy;(2) Interdepartmental Research Centre for Models and Information Analysis in Biomedical Systems (CISB), La Sapienza University of Rome, C.so Vittorio Emanuele II 244, 00186 Rome, Italy;(3) INFN, Sezione di Roma, P.le A. Moro 2, 00185 Rome, Italy |
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Abstract: | Background Natively unfolded proteins lack a well defined three dimensional structure but have important biological functions, suggesting
a re-assignment of the structure-function paradigm. To assess that a given protein is natively unfolded requires laborious
experimental investigations, then reliable sequence-only methods for predicting whether a sequence corresponds to a folded
or to an unfolded protein are of interest in fundamental and applicative studies. Many proteins have amino acidic compositions
compatible both with the folded and unfolded status, and belong to a twilight zone between order and disorder. This makes
difficult a dichotomic classification of protein sequences into folded and natively unfolded ones. In this work we propose
an operational method to identify proteins belonging to the twilight zone by combining into a consensus score good performing
single predictors of folding. |
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