Protein misfolding /

• Άλλοι συγγραφείς: Donev, Rossen (Επιμελητής έκδοσης)
• Μορφή: Ηλ. βιβλίο
• Γλώσσα: English
• Έκδοση: [Place of publication not identified] : Academic Press, 2020.
• Σειρά: Advances in protein chemistry and structural biology ; v. 118.
• Θέματα: Protein folding.; Protein Folding.; Electronic books.

Πίνακας περιεχομένων:

• 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
• 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
• 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
• 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