Integrity of H1 helix in prion protein revealed by molecular dynamic simulations to be especially vulnerable to changes in the relative orientation of H1 and its S1 flank.
Tseng, Chih-Yuan
Integrity of H1 helix in prion protein revealed by molecular dynamic simulations to be especially vulnerable to changes in the relative orientation of H1 and its S1 flank. [electronic resource] - European biophysics journal : EBJ Jun 2009 - 601-11 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1432-1017
10.1007/s00249-009-0414-4 doi
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Peptide Fragments--chemistry
Prions--chemistry
Protein Denaturation
Protein Stability
Protein Structure, Secondary
Integrity of H1 helix in prion protein revealed by molecular dynamic simulations to be especially vulnerable to changes in the relative orientation of H1 and its S1 flank. [electronic resource] - European biophysics journal : EBJ Jun 2009 - 601-11 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1432-1017
10.1007/s00249-009-0414-4 doi
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Peptide Fragments--chemistry
Prions--chemistry
Protein Denaturation
Protein Stability
Protein Structure, Secondary