Characterizing Protease Specificity: How Many Substrates Do We Need?

• Published in: PloS one Vol. 10; no. 11; p. e0142658
• Main Authors: Schauperl, Michael, Fuchs, Julian E, Waldner, Birgit J, Huber, Roland G, Kramer, Christian, Liedl, Klaus R
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 11.11.2015; Public Library of Science (PLoS)
• Subjects: Algorithms; Amino Acid Sequence; Amino acids; Analysis; Bayes Theorem; Bioinformatics; Cleavage; Computational Biology; Data points; Deoxyribonucleic acid; DNA; Drug Design; Drug development; Endopeptidases - chemistry; Endopeptidases - metabolism; Entropy (Information theory); Enzyme regulation; Estimates; Estimation; Factor Xa - chemistry; Humans; Innovations; Linear Models; Mathematical analysis; Mathematical models; Models, Biological; Numerical stability; Observations; Peptide Hydrolases - chemistry; Peptide Library; Peptides - chemistry; Pharmaceutical industry; Properties; Protease; Proteases; Proteinase; Proteins; Stability analysis; Statistical analysis; Statistical analysis of data; Statistical methods; Statistics; Substrate Specificity; Substrates; Technology application; Theory; Thrombin - chemistry; Trypsin - chemistry; Uncertainty; Tyrol (State in Austria); Austria; Singapore

Calculation of cleavage entropies allows to quantify, map and compare protease substrate specificity by an information entropy based approach. The metric intrinsically depends on the number of experimentally determined substrates (data points). Thus a statistical analysis of its numerical stability...