Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes

• Main Authors: Song J., Qin H., Lim L., Wei Y., Gupta G.
• Other Authors: BIOLOGY (NU)
• Format: Article
• Published: 2020
• Subjects: alpha synuclein; major sperm protein; melittin; membrane protein; unclassified drug; aging; alpha helix; Article; homeostasis; human; hydrogen bond; molecular interaction; molecular pathology; nuclear magnetic resonance; protein aggregation; protein conformation; protein degradation; protein determination; protein domain; protein expression; protein folding; protein function; protein homeostasis; protein stability; structure analysis; upregulation
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/174579
• Institution: National University of Singapore

10.12688/f1000research.2-221.v2