Proline isomerization effects in the amyloidogenic protein β2-microglobulin
Copyright policy )Proline isomerization effects in the amyloidogenic protein β2-microglobulin
The protein β2-microglobulin can aggregate in insoluble amyloid fibrils. By relying on extensive sampling simulations, we study the Pro32 isomerization as a possible triggering factor leading to structural modifications in β2-m.
- National Research Council Italy
- University of Modena and Reggio Emilia Italy
- King's College London United Kingdom
- Istituto Nanoscienze - Consiglio Nazionale delle Ricerche Italy
- University of Padua Italy
---, Proline, Protein Conformation, 500, Amyloidogenic Proteins, Hydrogen Bonding, Stereoisomerism, Dipeptides, Molecular Dynamics Simulation, 540, Amyloidogenic Proteins; Dipeptides; Humans; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Molecular Dynamics Simulation; Point Mutation; Proline; Protein Conformation; Stereoisomerism; beta 2-Microglobulin, Humans, Point Mutation, beta 2-Microglobulin, Hydrophobic and Hydrophilic Interactions
---, Proline, Protein Conformation, 500, Amyloidogenic Proteins, Hydrogen Bonding, Stereoisomerism, Dipeptides, Molecular Dynamics Simulation, 540, Amyloidogenic Proteins; Dipeptides; Humans; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Molecular Dynamics Simulation; Point Mutation; Proline; Protein Conformation; Stereoisomerism; beta 2-Microglobulin, Humans, Point Mutation, beta 2-Microglobulin, Hydrophobic and Hydrophilic Interactions
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