33,970 research outputs found
Prediction of protein-protein interactions using one-class classification methods and integrating diverse data
This research addresses the problem of prediction of protein-protein interactions (PPI)
when integrating diverse kinds of biological information. This task has been commonly
viewed as a binary classification problem (whether any two proteins do or do not interact)
and several different machine learning techniques have been employed to solve this
task. However the nature of the data creates two major problems which can affect results.
These are firstly imbalanced class problems due to the number of positive examples (pairs
of proteins which really interact) being much smaller than the number of negative ones.
Secondly the selection of negative examples can be based on some unreliable assumptions
which could introduce some bias in the classification results.
Here we propose the use of one-class classification (OCC) methods to deal with the task of
prediction of PPI. OCC methods utilise examples of just one class to generate a predictive
model which consequently is independent of the kind of negative examples selected; additionally
these approaches are known to cope with imbalanced class problems. We have
designed and carried out a performance evaluation study of several OCC methods for this
task, and have found that the Parzen density estimation approach outperforms the rest. We
also undertook a comparative performance evaluation between the Parzen OCC method
and several conventional learning techniques, considering different scenarios, for example
varying the number of negative examples used for training purposes. We found that the
Parzen OCC method in general performs competitively with traditional approaches and in
many situations outperforms them. Finally we evaluated the ability of the Parzen OCC
approach to predict new potential PPI targets, and validated these results by searching for
biological evidence in the literature
An empirical comparison of supervised machine learning techniques in bioinformatics
Research in bioinformatics is driven by the experimental data.
Current biological databases are populated by vast amounts of
experimental data. Machine learning has been widely applied to
bioinformatics and has gained a lot of success in this research
area. At present, with various learning algorithms available in the
literature, researchers are facing difficulties in choosing the best
method that can apply to their data. We performed an empirical
study on 7 individual learning systems and 9 different combined
methods on 4 different biological data sets, and provide some
suggested issues to be considered when answering the following
questions: (i) How does one choose which algorithm is best
suitable for their data set? (ii) Are combined methods better than
a single approach? (iii) How does one compare the effectiveness
of a particular algorithm to the others
Rapid design of LCC current-output resonant converters with reduced electrical stresses
The paper presents and validates a straightforward design methodology for realising LCC current-output resonant converters, with the aim of reducing tank currents, and hence, electrical stresses on resonant components. The scheme is ideally suited for inclusion in a rapid iterative design environment e.g. part of a graphical user interfac
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Characterisation of FAD-family folds using a machine learning approach
Flavin adenine dinucleotide (FAD) and its derivatives play a crucial role in
biological processes. They are major organic cofactors and electron carriers
in both enzymatic activities and biochemical pathways. We have analysed
the relationships between sequence and structure of FAD-containing proteins
using a machine learning approach. Decision trees were generated using the
C4.5 algorithm as a means of automatically generating rules from biological
databases (TOPS, CATH and PDB). These rules were then used as
background knowledge for an ILP system to characterise the four different
classes of FAD-family folds classified in Dym and Eisenberg (2001). These
FAD-family folds are: glutathione reductase (GR), ferredoxin reductase (FR),
p-cresol methylhydroxylase (PCMH) and pyruvate oxidase (PO). Each FADfamily
was characterised by a set of rules. The “knowledge patterns”
generated from this approach are a set of rules containing conserved sequence
motifs, secondary structure sequence elements and folding information.
Every rule was then verified using statistical evaluation on the measured
significance of each rule. We show that this machine learning approach is
capable of learning and discovering interesting patterns from large biological
databases and can generate “knowledge patterns” that characterise the FADcontaining
proteins, and at the same time classify these proteins into four
different families
The algebra of rewriting for presentations of inverse monoids
We describe a formalism, using groupoids, for the study of rewriting for
presentations of inverse monoids, that is based on the Squier complex
construction for monoid presentations. We introduce the class of pseudoregular
groupoids, an example of which now arises as the fundamental groupoid of our
version of the Squier complex. A further key ingredient is the factorisation of
the presentation map from a free inverse monoid as the composition of an
idempotent pure map and an idempotent separating map. The relation module of a
presentation is then defined as the abelianised kernel of this idempotent
separating map. We then use the properties of idempotent separating maps to
derive a free presentation of the relation module. The construction of its
kernel - the module of identities - uses further facts about pseudoregular
groupoids.Comment: 22 page
Multiple structural alignment for distantly related all b structures using TOPS pattern discovery and simulated annealing
Topsalign is a method that will structurally align diverse protein structures, for example, structural alignment of protein superfolds. All proteins within a superfold share the same fold but often have very low sequence identity and different biological and biochemical functions. There is often signi®cant structural diversity around the common scaffold of secondary structure elements of the fold. Topsalign uses topological descriptions of proteins. A pattern discovery algorithm identi®es equivalent secondary structure elements between a set of proteins and these are used to produce an initial multiple structure alignment. Simulated annealing is used to optimize the alignment. The output of Topsalign is a multiple structure-based sequence alignment and a 3D superposition of the structures. This method has been tested on three superfolds: the b jelly roll, TIM (a/b) barrel and the OB fold. Topsalign outperforms established methods on very diverse structures. Despite the pattern discovery working only on b strand secondary structure elements, Topsalign is shown to align TIM (a/b) barrel superfamilies, which contain both a helices and b strands
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Transient analysis and synthesis of linear circuits using constraint logic programming
In this paper describes the design of a transient analysis program for linear circuits and its implementation
in a Constraint Logic Programming language, CLP(R). The transient analysis program parses the input
circuit description into a network graph, analyses its semantic correctness and then performs the transient
analysis. The test results show that the program is at least 97% accurate when run at two decimal
places. We have also compared the performance of our program with a commercial package implemented
in an imperative language. The advantages of implementing the analysis program in a CLP language
include: quick construction and ease of maintenance. We also report on the synthesis of generation of a
circuit with given transient characteristics
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Multi-class protein fold classification using a new ensemble machine learning approach.
Protein structure classification represents an important process in understanding the associations
between sequence and structure as well as possible functional and evolutionary relationships.
Recent structural genomics initiatives and other high-throughput experiments have populated the
biological databases at a rapid pace. The amount of structural data has made traditional methods
such as manual inspection of the protein structure become impossible. Machine learning has been
widely applied to bioinformatics and has gained a lot of success in this research area. This work
proposes a novel ensemble machine learning method that improves the coverage of the classifiers
under the multi-class imbalanced sample sets by integrating knowledge induced from different base
classifiers, and we illustrate this idea in classifying multi-class SCOP protein fold data. We have
compared our approach with PART and show that our method improves the sensitivity of the
classifier in protein fold classification. Furthermore, we have extended this method to learning over
multiple data types, preserving the independence of their corresponding data sources, and show
that our new approach performs at least as well as the traditional technique over a single joined
data source. These experimental results are encouraging, and can be applied to other bioinformatics
problems similarly characterised by multi-class imbalanced data sets held in multiple data
sources
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Integrative machine learning approach for multi-class SCOP protein fold classification
Classification and prediction of protein structure has been a central research theme in structural bioinformatics. Due to the imbalanced distribution of proteins over multi SCOP classification, most discriminative machine learning suffers the well-known ‘False Positives ’ problem when learning over these types of problems. We have devised eKISS, an ensemble machine learning specifically designed to increase the coverage of positive examples when learning under multiclass imbalanced data sets. We have applied eKISS to classify 25 SCOP folds and show that our learning system improved over classical learning methods
Predicting protein function by machine learning on amino acid sequences – a critical evaluation
Copyright @ 2007 Al-Shahib et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.Background: Predicting the function of newly discovered proteins by simply inspecting their amino acid sequence is one of the major challenges of post-genomic computational biology, especially when done without recourse to experimentation or homology information. Machine learning classifiers are able to discriminate between proteins belonging to different functional classes. Until now, however, it has been unclear if this ability would be transferable to proteins of unknown function, which may show distinct biases compared to experimentally more tractable proteins. Results: Here we show that proteins with known and unknown function do indeed differ significantly. We then show that proteins from different bacterial species also differ to an even larger and very surprising extent, but that functional classifiers nonetheless generalize successfully across species boundaries. We also show that in the case of highly specialized proteomes classifiers from a different, but more conventional, species may in fact outperform the endogenous species-specific classifier. Conclusion: We conclude that there is very good prospect of successfully predicting the function of yet uncharacterized proteins using machine learning classifiers trained on proteins of known function
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