TAILIEUCHUNG - Báo cáo khoa học: Insufficient hydrogen-bond desolvation and prion-related disease

A structuring and eventual exclusion of water surrounding backbone hydrogen bonds takes place during protein fold-ing as hydrophobic residues cluster around such bonds. Taken as an average over all hydrogen bonds, the extent of desolvation is nearly a constant of motion, as revealed by re-examination of the longest all-atom trajectory with explicit solvent [ & (1998)Science 282, 740].Furthermore, this extent of desolvation is pre-served across native soluble proteins, except for cellular prion proteins | Eur. J. Biochem. 269 4165-4168 2002 FEBS 2002 doi PRIORITY PAPER Insufficient hydrogen-bond desolvation and prion-related disease Ariel Fernandez Institute for Biophysical Dynamics The University of Chicago Chicago IL USA A structuring and eventual exclusion of water surrounding backbone hydrogen bonds takes place during protein folding as hydrophobic residues cluster around such bonds. Taken as an average over all hydrogen bonds the extent of desolvation is nearly a constant of motion as revealed by re-examination of the longest all-atom trajectory with explicit solvent Y. Duan p. A. Kdlman 18 Science 282 740 . uutlhermore. this extent of desolvation IS preserved across native soluble proteins except for cellular prion proteins. Thus a phyiic o-ct-eniiv al pittLit e fl príon-related disease emerges. The epi ope for pooteOi-X binding the region undergoing vast conformational change and the trigger and locker for this change are inferred from the location of under-desolvated hydrogen bonds in the cellular prion protein. Keywords protein folding hydrogen bond backbone desolvation all-atom trajectory prions. The progressive structuring immobilization and ultimate removal of water surrounding the backbone hydrogen bonds HBs of a protein tum the latter into major determinants of protein folding and structure 1-5 . However to the best of my knowledge a systematic examination of evolving environments surrounding backbone HBs has been inherent stability of such bonds is essentially defined by the solvation free energy of the unbound reference state with its exposed backbone polar groups the amides and carbonyls 1-3 . Thus most of HB stability is brought about by the destabilization of the unbound state due to progressive removal of surrounding water from the backbone polar moieties. The inaccessibility of HBs to solvent takes place as the protein places hydrophobes around its backbone polar groups 1 during the folding process. .

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