Disulfide bridges remain intact while native insulin converts into amyloid fibrils

Amyloid fibrils are β-sheet-rich protein aggregates commonly found in the organs and tissues of patients with various amyloid-associated diseases. Understanding the structural organization of amyloid fibrils can be beneficial for the search of drugs to successfully treat diseases associated with pro...

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Veröffentlicht in:	PloS one 2012-06, Vol.7 (6), p.e36989-e36989
Hauptverfasser:	Kurouski, Dmitry, Washington, Jacqueline, Ozbil, Mehmet, Prabhakar, Rajeev, Shekhtman, Alexander, Lednev, Igor K
Format:	Artikel
Sprache:	eng
Schlagworte:	Acids Algorithms Amino Acid Sequence Amino acids Amino Acids - metabolism Amyloid - metabolism Animals Bioinformatics Biology Bonds (Securities) Cattle Chemical bonds Chemistry Deuterium Deuterium Exchange Measurement Diabetes therapy Disease Distributed processing Disulfide bonds Disulfides - metabolism Drugs Fibrils Free radicals Humans Hydration Hydrogen Hydrogen-deuterium exchange Insulin Insulin - chemistry Insulin - metabolism Magnetic resonance Magnetic Resonance Spectroscopy Medicine Molecular Dynamics Simulation Molecular Sequence Data Molecular structure NMR Nuclear magnetic resonance Nuclear magnetic resonance spectroscopy Organs Phenylalanine Polypeptides Protein folding Protein Multimerization Protein structure Protein Structure, Secondary Proteins Psittacula krameri Resonance Signal transduction Solutions Spectroscopy Studies Tissues Tyrosine
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