منابع مشابه
BLOMAP: An encoding of amino acids which improves signal peptide cleavage site prediction
Research on cleavage site prediction for signal peptides has focused mainly on the application of different classification algorithms to achieve improved prediction accuracies. This paper addresses the fundamental issue of amino acid encoding to present amino acid sequences in the most beneficial way for machine learning algorithms. A comparison of several standard encoding methods shows, that ...
متن کاملSequences beyond the cleavage site influence signal peptide function.
The earliest events in protein secretion include targeting to and translocation across the endoplasmic reticulum membrane. To dissect the mechanism by which signal sequences mediate translocation in eukaryotes, we are examining the behavior of fusion proteins and deletion mutants in cell-free systems. We demonstrate that the protein domain being translocated can have profound impact on the effi...
متن کاملSupport Vector Machine Prediction of Signal Peptide Cleavage Site Using a New Class of Kernels for Strings
A new class of kernels for strings is introduced. These kernels can be used by any kernel-based data analysis method, including support vector machines (SVM). They are derived from probabilistic models to integrate biologically relevant information. We show how to compute the kernels corresponding to several classical probabilistic models, and illustrate their use by building a SVM for the prob...
متن کاملSite-selective chemical cleavage of peptide bonds.
Site-selective cleavage of extremely unreactive peptide bonds is a very important chemical modification that provides invaluable information regarding protein sequence, and it acts as a modulator of protein structure and function for therapeutic applications. For controlled and selective cleavage, a daunting task, chemical reagents must selectively recognize or bind to one or more amino acid re...
متن کاملSignal peptide discrimination and cleavage site identification using SVM and NN
About 15% of all proteins in a genome contain a signal peptide (SP) sequence, at the N-terminus, that targets the protein to intracellular secretory pathways. Once the protein is targeted correctly in the cell, the SP is cleaved, releasing the mature protein. Accurate prediction of the presence of these short amino-acid SP chains is crucial for modelling the topology of membrane proteins, since...
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ژورنال
عنوان ژورنال: Genome Biology
سال: 2000
ISSN: 1474-760X
DOI: 10.1186/gb-2000-1-3-reports2054