Simulation study of the structure and dynamics of the Alzheimer's amyloid peptide congener in solution

Biophysical Journal

Volumn 80, Issue 1, 2001, Pages 31-44

  Massi, Francesca ^a   Peng, Jeff W ^b   Lee, Jonathan P ^a   Straub, John E ^a  

^a Boston University   (United States)

^b VERTEX PHARMACEUTICALS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; PEPTIDE;

ALZHEIMER DISEASE; AMYLOIDOSIS; ARTICLE; DIFFUSION; HYDRODYNAMICS; LIGHT SCATTERING; MOLECULAR STABILITY; NUCLEAR MAGNETIC RESONANCE; PROTEIN BINDING; SIMULATION; STATISTICAL ANALYSIS; VIBRATION;

EID: 0035133048     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)75993-0     Document Type: Article

References (32)

1. Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's-disease: Analysis of circular-dichroism spectra
2. Charmm: A program for macromolecular energy minimization and dynamics calculations
3. Activation barriers to structural transition determine deposition rates of Alzheimer's disease Aβ amyloid
4. In vitro growth of Alzheimer's disease beta-amyloid plaques displays first-order kinetics
5. Point substitution in the central hydrophobic cluster of a human β-amyloid congener disrupts peptide folding and abolishes plaque competence
6. Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
7. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein
8. Temperature dependence of amyloid β-protein fibrillization
9. A reductionist view of Alzheimer's disease
10. Interpretation of protein structures: Estimation of static accessibility
11. 1H NMR of Aβ amyloid peptide congeners in water solution. Conformational changes correlate with plaque competence
12. Model free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules: 1. Theory and range of validity
13. Model free approach to the interpretation of Nuclear Magnetic Resonance relaxation in macromolecules: 1. Analysis of experimental results
14. On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants
15. Kinetic theory of fibrillogenesis of amyloid β-protein
16. All-atom empirical potential for molecular modeling and dynamics studies of proteins
17. Brain amyloid: A physicochemical perspective
18. Mapping of the spectral densities of the N-H bond motions in eglin c using heteronuclear relaxation experiments
19. Frequency spectrum of NH bonds in eglin c from spectral density mapping at multiple fields
20. Internal motions in the molecular tumbling regime: Effect on NMR dipolar cross relaxation and interproton distance determination
21. Amyloid fibrillogenesis: Themes and variations
22. Alzheimer's disease: A central role for amyloid
23. A program for visualization of structure and dynamics of biomolecules and STO: A program for computing stochastic paths
24. Structural and kinetic features of amyloid β-protein fibrillogenesis
25. Deposition of monomeric, not oligomeric, Aβ mediates growth of Alzheimer's disease amyloid plaques in human brain preparations
26. Amyloid β-protein fibrillogenesis: Detection of a protofibrillar intermediate
27. Atomic solvation parameters applied to molecular dynamics of proteins in solution
28. The Alzheimer's peptide Aβ adopts a collapsed coil structure in water
29. Residual structure in the Alzheimer's disease peptide: Probing the origin of a central hydrophobic cluster