Cooperative hydrogen bonding in amyloid formation

Protein Science

Volumn 16, Issue 4, 2007, Pages 761-764

  Tsemekhman, Kiril ^a   Goldschmidt, Lukasz ^b   Eisenberg, David ^b   Baker, David ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Amyloid energetics; Density functional theory; GNNQQNY; Sup35

Indexed keywords

AMYLOID; PRION PROTEIN; PROTEIN SUP35; UNCLASSIFIED DRUG;

ARTICLE; CELL NUCLEUS; CHEMICAL STRUCTURE; DENSITY FUNCTIONAL THEORY; ENERGY TRANSFER; HYDROGEN BOND; KINETICS; MOLECULE; POLARIZATION; PRIORITY JOURNAL; QUANTUM CHEMISTRY;

AMYLOID; ELECTROSTATICS; HYDROGEN BONDING;

EID: 33947728761     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062609607     Document Type: Article

References (13)

1. Coulson, C.A. and Eisenberg, D. 1966. Interactions of H2O molecules in ice: The dipole moment of an H2Omolecule in ice. Proc. R. Soc. Lond. 291: 445.
2. Eisenberg, D. and Kauzmann, W. 2005. The structure and properties of water. Oxford Classic Texts, Oxford, UK.
3. Hol, W. 1985. Effects of the α-helix dipole upon the functioning and structure of proteins and peptides. Adv. Biophys. 19: 133-165.
4. Kresse, G. and Hafner, J. 1993. Ab initio molecular dynamics for liquid metals. Phys. Rev. B 47: 558-561.
5. Krimm, S. 2001. A polarizable electrostatic model of the N-methylacetamide dimer. J. Comput. Chem. 22: 1933-1943.
6. Lomakin, A., Chung, D.S., Benedek, G.B., Kirschner, D.A., and Teplow, D. 1996. On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants. Proc. Natl. Acad. Sci. 93: 1125-1129.
7. Ma, B. and Nussinov, R. 2006. Simulations as analytical tools to understand protein aggregation and predict amyloid conformation. Curr. Opin. Chem. Biol. 10: 445-452.
8. Makin, O.S. and Serpell, L.C. 2005. Structures for amyloid fibrils. FEBS J. 272: 5950-5961.
9. Morozov, A., Kortemme, T., Tsemekhman, K., and Baker, D. 2004. Close agreement between the orientation dependence of hydrogen bonds observed in protein structures and quantum mechanical calculations. Proc. Natl. Acad. Sci. 101: 6946-6951.
10. Nelson, R., Sawaya, M.R., Balbirnie, M., Madsen, A.Ø., Riekel, C., Grothe, R., and Eisenberg, D. 2005. Structure of the cross-β spine of amyloid-like fibrils. Nature 435: 773-778.
11. Parr, R. and Yang, W. 1989. Density functional theory of atoms and molecules. Oxford University Press, Oxford, UK.
12. Pellarin, P. and Caflisch, A. 2006. Interpreting the aggregation kinetics of amyloid peptides. J. Mol. Biol. 360: 882-892.
13. Zheng, J., Ma, B., Tsai, C.J., and Nussinov, R. 2006. Structural stability and dynamics of an amyloid-forming peptide GNNQQNY from the yeast prion sup-35. Biophys. J. 91: 824-833.