Solution NMR insights into dynamic supramolecular assemblies of disordered amyloidogenic proteins.

Munari, Francesca; D'Onofrio, Mariapina; Assfalg, Michael

Munari, Francesca; D'Onofrio, Mariapina; Assfalg, Michael.

Affiliation

Munari F; Department of Biotechnology, University of Verona, Strada Le Grazie 15, 37134, Verona, Italy.
D'Onofrio M; Department of Biotechnology, University of Verona, Strada Le Grazie 15, 37134, Verona, Italy.
Assfalg M; Department of Biotechnology, University of Verona, Strada Le Grazie 15, 37134, Verona, Italy. Electronic address: michael.assfalg@univr.it.

Arch Biochem Biophys ; 683: 108304, 2020 04 15.

Article in En | MEDLINE | ID: mdl-32097611

Subject(s)

Amyloidogenic Proteins/chemistry; Intrinsically Disordered Proteins/chemistry; Magnetic Resonance Spectroscopy; Adsorption; Humans; Huntingtin Protein/chemistry; Kinetics; Macromolecular Substances; Peptides/chemistry; Protein Binding; Protein Conformation; tau Proteins/chemistry

Key words

Aggregation; Amyloidogenic protein; Biomolecular condensate; Intrinsically disordered protein; NMR spectroscopy; Supramolecular assembly

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Magnetic Resonance Spectroscopy / Amyloidogenic Proteins / Intrinsically Disordered Proteins Limits: Humans Language: En Journal: Arch Biochem Biophys Year: 2020 Type: Article Affiliation country: Italy

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