From Protein Structure to Function with Bioinformatics
(Sprache: Englisch)
Proteins lie at the heart of almost all biological processes and have an incredibly wide range of activities. Central to the function of all proteins is their ability to adopt, stably or sometimes transiently, structures that allow for interaction with...
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Proteins lie at the heart of almost all biological processes and have an incredibly wide range of activities. Central to the function of all proteins is their ability to adopt, stably or sometimes transiently, structures that allow for interaction with other molecules. An understanding of the structure of a protein can therefore lead us to a much improved picture of its molecular function. This realisation has been a prime motivation of recent Structural Genomics projects, involving large-scale experimental determination of protein structures, often those of proteins about which little is known of function. These initiatives have, in turn, stimulated the massive development of novel methods for prediction of protein function from structure. Since model structures may also take advantage of new function prediction algorithms, the first part of the book deals with the various ways in which protein structures may be predicted or inferred, including specific treatment of membrane and intrinsically disordered proteins. A detailed consideration of current structure-based function prediction methodologies forms the second part of this book, which concludes with two chapters, focusing specifically on case studies, designed to illustrate the real-world application of these methods. With bang up-to-date texts from world experts, and abundant links to publicly available resources, this book will be invaluable to anyone who studies proteins and the endlessly fascinating relationship between their structure and function.
Klappentext zu „From Protein Structure to Function with Bioinformatics “
Proteins lie at the heart of almost all biological processes and have an incredibly wide range of activities. Central to the function of all proteins is their ability to adopt, stably or sometimes transiently, structures that allow for interaction with other molecules. An understanding of the structure of a protein can therefore lead us to a much improved picture of its molecular function. This realisation has been a prime motivation of recent Structural Genomics projects, involving large-scale experimental determination of protein structures, often those of proteins about which little is known of function. These initiatives have, in turn, stimulated the massive development of novel methods for prediction of protein function from structure. Since model structures may also take advantage of new function prediction algorithms, the first part of the book deals with the various ways in which protein structures may be predicted or inferred, including specific treatment of membrane and intrinsically disordered proteins. A detailed consideration of current structure-based function prediction methodologies forms the second part of this book, which concludes with two chapters, focusing specifically on case studies, designed to illustrate the real-world application of these methods. With bang up-to-date texts from world experts, and abundant links to publicly available resources, this book will be invaluable to anyone who studies proteins and the endlessly fascinating relationship between their structure and function.
Inhaltsverzeichnis zu „From Protein Structure to Function with Bioinformatics “
Table of ContentsPart 1: Generating and inferring structures 1 Ab initio protein structure prediction1.1 Introduction1.2 Energy functions1.2.1 Physics-based energy functions1.2.2 Knowledge-based energy function combined with fragments1.3 Conformational search methods1.3.1 Monte Carlo simulations1.3.2 Molecular dynamics1.3.3 Genetic algorithm1.3.4 Mathematical optimization1.4 Model selection1.4.1 Physics-based energy function1.4.2 Knowledge-based energy function1.4.3 Sequence-structure compatibility function1.4.4 Clustering of decoy structure1.5 Remarks and discussion2 Fold Recognition 2.1 Introduction2.1.1 The importance of blind trials: the CASP competition2.1.2 Ab initio structure prediction versus homology modelling2.1.3 The limits of fold space2.1.4 A note on terminology: 'threading' and 'fold recognition'2.2 Threading2.2.1 Knowledge-based potentials2.2.2 Finding an alignment2.2.3 Heuristics for alignment2.3 Remote homology detection without threading2.3.1 Using predicted structural features2.3.2 Sequence profiles and hidden Markov models2.3.3 Fold Classification and Support Vector Machines2.3.4 Consensus approaches2.3.5 Traversing the homology network2.4 Alignment accuracy, model quality and statistical significance2.4.1 Algorithms for alignment generation and assessment2.4.2 Estimation of statistical significance2.5 Tools for fold recognition on the web2.6 The future3 Comparative protein structure modelling3.1 Introduction3.1.1 Structure determines function3.1.2 Sequences, structures, structural genomics3.1.3 Approaches to protein structure prediction3.2 Steps in comparative protein structure modelling3.2.1 Searching for structures related to the target sequence3.2.2 Selecting templates3.2.3 Sequence to structure alignment3.2.4 Modelbuilding3.2.5 Model evaluation3.3 Performance of comparative modelling3.3.1 Accuracy of methods3.3.2 Errors in comparative models3.4 Applications of comparative modelling3.4.1 Modelling of individual proteins3.4.2 Comparative
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modelling and the Protein Structure Initiative3.5 Summary4 Membrane protein structure prediction4.1 Introduction4.2 Structural classes4.2.1 Alpha-helical bundles4.2.2 Beta-barrels4.3 Membrane proteins are difficult to crystallise4.4 Databases4.5 Multiple sequence alignments4.6 Transmembrane protein topology prediction4.6.1 Alpha-helical proteins4.6.2 Beta-barrel proteins4.6.3 Whole genome analysis4.6.4 Data sets, homology, accuracy and cross-validation4.7 3D structure prediction4.8 Future developments5 Bioinformatics approaches to the structure and function of intrinsically disordered proteins5.1 The concept of protein disorder5.2 Sequence features of IDPs5.2.1 The unusual amino acid composition of IDPs5.2.2 Sequence patterns of IDPs5.2.3 Low sequence complexity and disorder5.3 Prediction of disorder5.3.1 Prediction of low-complexity regions5.3.2 Charge-hydropathy plot5.3.3 Propensity-based predictors5.3.4 Predictors based on the lack of secondary structure5.3.5 Machine learning algorithms5.3.6 Prediction based on contact potentials5.3.7 A reduced alphabet suffices to predict disorder5.3.8 Comparison of disorder prediction methods5.4 Functional classification of IDPs5.4.1 Gene Ontology-based functional classification of IDPs5.4.2 Classification of IDPs based on their mechanism of action5.4.3 Function-related structural elements in IDPs5.5 Prediction of the function of IDPs5.5.1 Correlation of disorder pattern and function5.5.2 Predicting short recognition motifs in IDRs5.5.3 Prediction of MoRFs5.5.4 Combination of information on sequence and disorder:
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Bibliographische Angaben
- 2008, XVI, 328 Seiten, Maße: 16,1 x 24,3 cm, Gebunden, Englisch
- Herausgegeben: Daniel John Rigden
- Verlag: Springer Netherland
- ISBN-10: 1402090579
- ISBN-13: 9781402090578
Sprache:
Englisch
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