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In this study, we propose a new method to predict hairpins in proteins and its evaluation based on the support vector machine. Different from previous methods, new feature representation scheme based on auto covariance is adopted. We also investigate two structure properties of proteins (protein secondary structure and residue conformation propensity), and examine their effects on prediction. Moreover, we employ an ensemble classifier approach based on the majority voting to improve prediction accuracy on hairpins. Experimental results on a dataset of 1926 protein chains show that our approach outperforms those previously published in the literature, which demonstrates the effectiveness of the proposed method.
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http://dx.doi.org/10.2174/092986610791760333 | DOI Listing |
Comput Struct Biotechnol J
December 2024
Clinical Physiology/Nutritional Medicine, Department of Gastroenterology, Rheumatology and Infectious Diseases, Charité - Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Hindenburgdamm 30, 12203 Berlin, Germany.
The pore-forming enterotoxin (CPE), a common cause of foodborne diseases, facilitates Ca influx in enterocytes, leading to cell damage. Upon binding to certain claudins (e.g.
View Article and Find Full Text PDFMethods Mol Biol
November 2024
Department of Computer Science, College of Engineering, Virginia Commonwealth University, Virginia, VA, USA.
The secondary structures (SSs) and supersecondary structures (SSSs) underlie the three-dimensional structure of proteins. Prediction of the SSs and SSSs from protein sequences enjoys high levels of use and finds numerous applications in the development of a broad range of other bioinformatics tools. Numerous sequence-based predictors of SS and SSS were developed and published in recent years.
View Article and Find Full Text PDFComput Struct Biotechnol J
December 2024
Institut für Physikalische Biologie, Heinrich Heine University Düsseldorf, 40204 Düsseldorf, Germany.
β-Structure-rich amyloid fibrils are hallmarks of several diseases, including Alzheimer's (AD), Parkinson's (PD), and type 2 diabetes (T2D). While amyloid fibrils typically consist of parallel β-sheets, the anti-parallel β-hairpin is a structural motif accessible to amyloidogenic proteins in their monomeric and oligomeric states. Here, to investigate implications of β-hairpins in amyloid formation, potential β-hairpin-forming amyloidogenic segments in the human proteome were predicted based on sequence similarity with β-hairpins previously observed in Aβ, α-synuclein, and islet amyloid polypeptide, amyloidogenic proteins associated with AD, PD, and T2D, respectively.
View Article and Find Full Text PDFBiomacromolecules
November 2023
School of Physics and Astronomy, University of Leeds, Leeds, United Kingdom, LS2 9JT.
Fundamental understanding of the structure and assembly of nanoscale building blocks is crucial for the development of novel biomaterials with defined architectures and function. However, accessing self-consistent structural information across multiple length scales is challenging. This limits opportunities to exploit atomic scale interactions to achieve emergent macroscale properties.
View Article and Find Full Text PDFPeerJ
August 2023
Eye Institute, Eye and ENT Hospital, College of Medicine, Fudan University, Shanghai, China.