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Advances in protein chemistry and structural biology. volume 118, Protein misfolding /

Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Donev, Rossen (Editor )
Formato: Electrónico eBook
Idioma:Inglés
Publicado: London ; San Diego : Academic Press, 2020.
Edición:First edition.
Colección:Advances in protein chemistry and structural biology ; v. 118.
Temas:
Acceso en línea:Texto completo

MARC

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245 0 0 |a Advances in protein chemistry and structural biology.  |n volume 118,  |p Protein misfolding /  |c edited by Rossen Donev. 
246 3 |a Protein misfolding 
250 |a First edition. 
264 1 |a London ;  |a San Diego :  |b Academic Press,  |c 2020. 
264 4 |c �2020 
300 |a 1 online resource 
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490 1 |a Advances in protein chemistry and structural biology ;  |v volume 118 
505 0 |a Front Cover -- Protein Misfolding -- Protein Misfolding -- Copyright -- Contents -- Contributors -- One -- Theoretical and computational advances in protein misfolding -- 1. Introduction -- 2. Mechanism of protein misfolding -- 3. Simulations: atomistic and coarse grained models -- 4. Atomistic simulations of early-stages monomers, small oligomers and end products of aggregation -- 5. Coarse grained models -- 6. Conclusions -- Acknowledgments -- References -- Two -- Combining molecular dynamics simulations and experimental analyses in protein misfolding -- 1. Introduction 
505 8 |a 2. Basic concepts of protein misfolding and aggregation -- 3. Biophysical analyses of protein misfolding -- 3.1 X-ray diffraction and small-angle X-ray scattering -- 3.2 Nuclear magnetic resonance analyses -- 3.3 Transmission electron microscopy and cryomicroscopy -- 3.4 Atomic force microscopy -- 3.5 Optical characterization -- 3.6 Mass-spectrometry -- 4. Molecular simulations of misfolding proteins -- 4.1 Atomistic modeling of proteins -- 4.2 Force fields for protein and water models -- 4.3 The challenges of system size and simulation time, and alternative approaches 
505 8 |a 4.4 Analysis of molecular dynamics trajectories -- 5. Integrative approaches in understanding misfolding and aggregation -- 5.1 Effects of mutations, truncations and insertions on protein structure and stability -- 5.2 Intermediate states, oligomers, and molecular basis of aggregation -- 5.3 Influence of extrinsic factors -- 6. Open questions and challenges -- Acknowledgments -- References -- Three -- Mass spectrometric approaches for profiling protein folding and stability -- 1. Introduction -- 2. Terminology -- 3. Quantitation in mass spectrometry -- 3.1 Spectral counts 
505 8 |a 3.2 Label free quantification -- 3.3 Targeted proteomics -- 3.4 Stable isotopes -- 3.5 Isobaric tags -- 4. Fractionation methods for characterizing the destabilized proteome -- 4.1 Thermal destabilization -- 4.2 Isolation of aggresomes -- 4.3 Conformational antibodies -- 5. Enzymatic methods for identifying protein stability -- 5.1 Limited proteolysis -- 5.2 Ubiquitinylation -- 6. Exploiting chemical reactivity to characterize protein stability -- 6.1 Hydrogen-deuterium exchange -- 6.2 FPOP -- 6.3 SPROX -- 6.4 Electrophilic profiling -- 6.5 Crosslinking and mass spectrometry (XL-MS) -- 7. Summary 
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700 1 |a Donev, Rossen,  |e editor. 
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