Protein Misfolding §

Group: 4 #group-4

Relations §

• Fold Resistance: Proteins with low fold resistance are more susceptible to misfolding, which can lead to the formation of non-functional or toxic protein aggregates.
• Disulfide Bridges: Improper formation or breakage of disulfide bridges can lead to protein misfolding, which is associated with various diseases, such as neurodegenerative disorders and certain cancers.
• Alzheimer’s Disease: Misfolding and aggregation of proteins like amyloid-beta are implicated in Alzheimer’s disease.
• Prion Diseases: Prion diseases, such as Creutzfeldt-Jakob disease, are caused by misfolded prion proteins.
• Protein Aggregation: Protein misfolding can lead to the formation of protein aggregates, which can be toxic to cells.
• Prions: Prions are infectious misfolded protein aggregates that can propagate their abnormal conformation to other proteins, causing neurodegenerative diseases.
• Protein Folding Landscapes: Rugged and frustrated protein folding landscapes can lead to protein misfolding and aggregation.
• Chaperone Proteins: Chaperone proteins assist in proper protein folding and can prevent misfolding.
• Molecular Chaperones: Molecular chaperones help prevent protein misfolding, which can lead to the formation of toxic protein aggregates.
• Amyloid Fibrils: Misfolded proteins can form insoluble amyloid fibrils, which are associated with various diseases.
• Parkinson’s Disease: Misfolding and aggregation of alpha-synuclein protein are linked to Parkinson’s disease.
• Amyloid Fibrils: Amyloid fibrils are insoluble protein aggregates associated with various diseases, such as Alzheimer’s and Parkinson’s.
• Folding in Nature: Improper protein folding can lead to various diseases and disorders.
• Folding in Biology: Protein misfolding can lead to the formation of abnormal structures and is associated with various diseases.
• Protein Folding Mechanisms: Misfolding of proteins can lead to the formation of insoluble aggregates, which are associated with various diseases.