Breakdown of supersaturation barrier links protein folding to amyloid formation

• Published in: Communications biology Vol. 4; no. 1; p. 120
• Main Authors: Noji, Masahiro, Samejima, Tatsushi, Yamaguchi, Keiichi, So, Masatomo, Yuzu, Keisuke, Chatani, Eri, Akazawa-Ogawa, Yoko, Hagihara, Yoshihisa, Kawata, Yasushi, Ikenaka, Kensuke, Mochizuki, Hideki, Kardos, József, Otzen, Daniel E., Bellotti, Vittorio, Buchner, Johannes, Goto, Yuji
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 26.01.2021; Nature Publishing Group; Nature Portfolio
• Subjects: 101/47; 631/45/470/2284; 631/57/2269; Agitation; alpha-Synuclein - chemistry; alpha-Synuclein - metabolism; Amino acid sequence; Amino Acid Sequence - physiology; Amyloid - chemistry; Amyloid - metabolism; Amyloidogenesis; Amyloidosis - etiology; Amyloidosis - metabolism; Biology; Biomedical and Life Sciences; Chemical Precipitation; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - metabolism; Fibrils; Free energy; High temperature; Humans; Intrinsically Disordered Proteins - chemistry; Intrinsically Disordered Proteins - metabolism; Islet Amyloid Polypeptide - chemistry; Islet Amyloid Polypeptide - metabolism; Life Sciences; Osmolar Concentration; Protein Aggregation, Pathological - etiology; Protein Aggregation, Pathological - metabolism; Protein Conformation; Protein Folding; Protein Multimerization - physiology; Protein structure; Self-assembly; tau Proteins - chemistry; tau Proteins - metabolism; Thermodynamics

The thermodynamic hypothesis of protein folding, known as the “Anfinsen’s dogma” states that the native structure of a protein represents a free energy minimum determined by the amino acid sequence. However, inconsistent with the Anfinsen’s dogma, globular proteins can misfold to form amyloid fibril...