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200116s2020 xx o 000 0 eng d |
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|a OPELS
|b eng
|e rda
|e pn
|c OPELS
|d EBLCP
|d OCLCF
|d OHS
|d OCLCO
|d YDX
|d UKMGB
|d GrThAP
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|a 019654575
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|a 1136544269
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|a 9780128177501
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|z (OCoLC)1136544269
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|a Protein misfolding /
|c edited by Rossen Donev.
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|a [Place of publication not identified] :
|b Academic Press,
|c 2020.
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|a 1 online resource.
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|a text
|b txt
|2 rdacontent
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|a online resource
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|a Advances in protein chemistry and structural biology ;
|v volume 118
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|a Title details screen.
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|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
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|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
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|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
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|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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|a Protein folding.
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|a Protein Folding.
|0 (DNLM)D017510
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|a Protein folding.
|2 fast
|0 (OCoLC)fst01079687
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|a Electronic books.
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|a Electronic books.
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|a Donev, Rossen,
|e editor.
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|c Original
|z 0128177500
|z 9780128177501
|w (OCoLC)1108532687
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| 830 |
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|a Advances in protein chemistry and structural biology ;
|v v. 118.
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4 |
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|3 ScienceDirect
|u https://www.sciencedirect.com/science/bookseries/18761623/118
|z Full Text via HEAL-Link
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