Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins

Journal of Biological Chemistry

Volumn 286, Issue 24, 2011, Pages 21796-21805

  Iwasa, Hisanori ^a   Meshitsuka, Shunsuke ^b   Hongo, Kunihiro ^a,b   Mizobata, Tomohiro ^a,b   Kawata, Yasushi ^a,b  

^a TOTTORI UNIVERSITY   (Japan)

^b TOTTORI UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBRIL; AMYLOID FIBRIL FORMATION; ASPARTIC ACIDS; CHAPERONIN; DEAMIDATION; DISORDERED PROTEINS; DISORDERED STATE; FIBRIL FORMATION; FOLDING REACTIONS; GUANIDINE HYDROCHLORIDE; MASS SPECTROSCOPY; MODEL SYSTEM; MOLECULAR CHAPERONES; PEPTIDE BONDS; STRUCTURAL CHANGE;

AMINO ACIDS; ESCHERICHIA COLI; GLYCOPROTEINS; MASS SPECTROMETRY; NEURODEGENERATIVE DISEASES; POLYPEPTIDES;

PROTEINS;

AMYLOID; ASPARAGINE; BACTERIAL PROTEIN; CHAPERONE; GLYCINE; ISOASPARTIC ACID; PROTEIN GROES; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; DEAMINATION; ESCHERICHIA COLI; MASS SPECTROMETRY; MUTATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; STRUCTURE ANALYSIS;

ALANINE; AMINO ACID SEQUENCE; AMYLOID; ASPARAGINE; ASPARTIC ACID; CHAPERONIN 10; ESCHERICHIA COLI; GUANIDINE; MAGNETIC RESONANCE SPECTROSCOPY; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDES; PROTEIN BINDING; PROTEIN CONFORMATION;

ESCHERICHIA COLI;

EID: 79958723000     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.228445     Document Type: Article

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