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Data Mining Techniques for the Life Sciences

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Cover of 'Data Mining Techniques for the Life Sciences'

Table of Contents

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    Book Overview
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    Chapter 1 Data Mining Techniques for the Life Sciences
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    Chapter 2 Protein Structure Databases.
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    Chapter 3 The MIntAct Project and Molecular Interaction Databases.
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    Chapter 4 Applications of Protein Thermodynamic Database for Understanding Protein Mutant Stability and Designing Stable Mutants.
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    Chapter 5 Classification and Exploration of 3D Protein Domain Interactions Using Kbdock.
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    Chapter 6 Data Mining of Macromolecular Structures.
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    Chapter 7 Criteria to Extract High-Quality Protein Data Bank Subsets for Structure Users.
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    Chapter 8 Homology-Based Annotation of Large Protein Datasets.
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    Chapter 9 Data Mining Techniques for the Life Sciences
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    Chapter 10 Improving the Accuracy of Fitted Atomic Models in Cryo-EM Density Maps of Protein Assemblies Using Evolutionary Information from Aligned Homologous Proteins.
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    Chapter 11 Systematic Exploration of an Efficient Amino Acid Substitution Matrix: MIQS.
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    Chapter 12 Promises and Pitfalls of High-Throughput Biological Assays.
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    Chapter 13 Data Mining Techniques for the Life Sciences
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    Chapter 14 Predicting Conformational Disorder.
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    Chapter 15 Classification of Protein Kinases Influenced by Conservation of Substrate Binding Residues.
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    Chapter 16 Spectral-Statistical Approach for Revealing Latent Regular Structures in DNA Sequence.
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    Chapter 17 Protein Crystallizability.
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    Chapter 18 Data Mining Techniques for the Life Sciences
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    Chapter 19 Data Mining Techniques for the Life Sciences
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    Chapter 20 Functional Analysis of Metabolomics Data.
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    Chapter 21 Data Mining Techniques for the Life Sciences
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    Chapter 22 A Broad Overview of Computational Methods for Predicting the Pathophysiological Effects of Non-synonymous Variants.
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    Chapter 23 Recommendation Techniques for Drug-Target Interaction Prediction and Drug Repositioning.
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    Chapter 24 Protein Residue Contacts and Prediction Methods.
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    Chapter 25 The Recipe for Protein Sequence-Based Function Prediction and Its Implementation in the ANNOTATOR Software Environment.
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    Chapter 26 Data Mining Techniques for the Life Sciences
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    Chapter 27 Data Mining Techniques for the Life Sciences
Attention for Chapter 4: Applications of Protein Thermodynamic Database for Understanding Protein Mutant Stability and Designing Stable Mutants.
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Chapter title
Applications of Protein Thermodynamic Database for Understanding Protein Mutant Stability and Designing Stable Mutants.
Chapter number 4
Book title
Data Mining Techniques for the Life Sciences
Published in
Methods in molecular biology, January 2016
DOI 10.1007/978-1-4939-3572-7_4
Pubmed ID
Book ISBNs
978-1-4939-3570-3, 978-1-4939-3572-7
Authors

M. Michael Gromiha, P. Anoosha, Liang-Tsung Huang

Editors

Oliviero Carugo, Frank Eisenhaber

Abstract

Protein stability is the free energy difference between unfolded and folded states of a protein, which lies in the range of 5-25 kcal/mol. Experimentally, protein stability is measured with circular dichroism, differential scanning calorimetry, and fluorescence spectroscopy using thermal and denaturant denaturation methods. These experimental data have been accumulated in the form of a database, ProTherm, thermodynamic database for proteins and mutants. It also contains sequence and structure information of a protein, experimental methods and conditions, and literature information. Different features such as search, display, and sorting options and visualization tools have been incorporated in the database. ProTherm is a valuable resource for understanding/predicting the stability of proteins and it can be accessed at http://www.abren.net/protherm/ . ProTherm has been effectively used to examine the relationship among thermodynamics, structure, and function of proteins. We describe the recent progress on the development of methods for understanding/predicting protein stability, such as (1) general trends on mutational effects on stability, (2) relationship between the stability of protein mutants and amino acid properties, (3) applications of protein three-dimensional structures for predicting their stability upon point mutations, (4) prediction of protein stability upon single mutations from amino acid sequence, and (5) prediction methods for addressing double mutants. A list of online resources for predicting has also been provided.

Mendeley readers

The data shown below were compiled from readership statistics for 21 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 1 5%
Unknown 20 95%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 6 29%
Researcher 4 19%
Student > Master 3 14%
Student > Postgraduate 2 10%
Professor 2 10%
Other 3 14%
Unknown 1 5%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 6 29%
Agricultural and Biological Sciences 5 24%
Computer Science 2 10%
Immunology and Microbiology 2 10%
Chemistry 2 10%
Other 2 10%
Unknown 2 10%