Dynamics of an intrinsically disordered protein reveal metastable conformations that potentially seed aggregation

Engineering & Materials Science

• Conformations 86%
• Seed 70%
• Peptides 67%
• Proteins 62%
• Agglomeration 59%
• Monomers 40%
• Nucleation 35%
• Amyloid 29%
• Cell death 25%
• Oligomers 24%
• Insulin 23%
• Free energy 20%
• Molecular dynamics 19%
• Medical problems 18%
• Deposits 16%
• Geometry 10%
• Computer simulation 9%

Medicine & Life Sciences

• Intrinsically Disordered Proteins 100%
• Seeds 70%
• Peptides 43%
• Molecular Dynamics Simulation 25%
• Hydrophobic and Hydrophilic Interactions 25%
• Amyloid Plaques 25%
• Amyloid 21%
• Population 17%
• Cell Death 17%
• Type 2 Diabetes Mellitus 17%
• Kinetics 16%
• Insulin 15%
• Proteins 8%

Chemical Compounds

• Peptide 39%
• Nucleation 37%
• Protein 28%
• Amyloid Fibril 27%
• Monomer 26%
• Apoptotic 26%
• Hydrophobic Surface 24%
• Cell Death 24%
• Secondary Structure 20%
• Oligomer 18%
• Gibbs Free Energy 17%
• Molecular Dynamics 16%
• Simulation 14%
• Solvent 10%
• Amount 9%
• Time 8%