Structure and Function of Intrinsically Disordered Proteins
The existence and functioning of intrinsically disordered proteins (IDPs) challenge the classical structure-function paradigm that equates function with a well-defined 3D structure. Uncovering the disordered complement of proteomes and understanding their functioning can extend the structure-function paradigm to herald new breakthroughs in drug dev
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Contents
Chapter 1 Principles of Protein Structure and Function
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1 |
Chapter 2 A Brief History of Protein Disorder
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21 |
Chapter 3 Indirect Techniques for Recognizing and Characterizing Protein Disorder
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31 |
Chapter 4 Hydrodynamic Techniques
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43 |
Chapter 5 Spectroscopic Techniques for Characterizing Disorder
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55 |
Chapter 6 Nuclear Magnetic Resonance
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73 |
Chapter 7 Proteomic Approaches for the Identification of IDPs
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85 |
Chapter 8 IDPs under Conditions Approaching In Vivo
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91 |
Chapter 11 Biological Processes Enriched in Disorder
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143 |
Chapter 12 Molecular Functions of Disordered Proteins
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163 |
Chapter 13 Evolution and Prevalence of Disorder
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189 |
Chapter 14 Extension of the StructureFunction Paradigm
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205 |
Chapter 15 Structural Disorder and Disease
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237 |
References
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265 |
313 | |
Back cover
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333 |
Other editions - View all
Structure and Function of Intrinsically Disordered Proteins Peter Tompa,Alan Fersht No preview available - 2009 |
Common terms and phrases
Acad activity amino acids amyloid basic binding Biochem Biochemistry bioinformatic Biol C-terminal calpastatin cell chaperone Chapter 12 characterized Chem complex conformational Copyright correlation CREB Csizmok Cyclin denatured disease disordered proteins disordered regions domain Dunker dynamics entropic enzyme eukaryotic example Figure flexibility fluorescence formation fully disordered function Fuxreiter gene genome globular proteins helical helix HSQC hydrophobic IDPs IDRs induced folding inhibitor interactions intrinsically disordered involved kinase linker MDM2 mechanism molecular molecules motifs mutations Natl nuclear observed ordered proteins partner peptide phosphorylation polypeptide chain PPII predicted disorder predictors prion Proc proteasome protein disorder protein folding proteome random coil receptor recognition regulation repeat Reproduced with permission residues resonance ribosomal SAXS secondary structural elements secondary structure Section securin segments sequence signaling spectroscopy structural disorder studies substrate subunits suggested targets tau protein tion Tompa transcription factors transient ubiquitination unfolded Uversky whereas yeast