Structure analysis of an amyloid-forming model peptide by a systematic glycine and proline scan

Biomacromolecules

Volumn 12, Issue 8, 2011, Pages 2988-2996

  Gerling, Ulla I M ^a   Brandenburg, Enrico ^a   Berlepsch, Hans V ^a   Pagel, Kevin ^b   Koksch, Beate ^a  

^a FREIE UNIVERSITÄT BERLIN   (Germany)

^b FRITZ HABER INSTITUT DER MAX PLANCK GESELLSCHAFT   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALTERNATIVE APPROACH; AMYLOID FIBRIL; AMYLOID STRUCTURES; COMMON FEATURES; CONFORMATIONAL TRANSITIONS; FLUORESCENCE STAINING; HELICAL STATE; HIGH-RESOLUTION TECHNIQUES; INTERNAL ARCHITECTURE; MARGINAL EFFECTS; MODEL PEPTIDES; MOLECULAR ARCHITECTURE; NMR AND X-RAY; PEPTIDE SEQUENCES; STRUCTURAL MODELS; STRUCTURE ANALYSIS; THIOFLAVIN T;

CIRCULAR DICHROISM SPECTROSCOPY; CONFORMATIONS; DICHROISM; GLYCOPROTEINS; MODEL STRUCTURES; NEURODEGENERATIVE DISEASES; PEPTIDES; TRANSMISSION ELECTRON MICROSCOPY; X RAY CRYSTALLOGRAPHY;

AMINO ACIDS;

AMINO ACID; AMYLOID; AMYLOID BETA PROTEIN; GLYCINE; PROLINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; DEGENERATIVE DISEASE; FIBER; NUCLEAR MAGNETIC RESONANCE; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN INTERACTION; PROTEIN STRUCTURE; SOLUBILITY; X RAY CRYSTALLOGRAPHY;

AMYLOID; CRYSTALLOGRAPHY, X-RAY; GLYCINE; MICROSCOPY, ATOMIC FORCE; MICROSCOPY, ELECTRON, TRANSMISSION; MODELS, CHEMICAL; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROLINE; PROTEIN CONFORMATION;

EID: 80051512866     PISSN: 15257797     EISSN: 15264602     Source Type: Journal    
DOI: 10.1021/bm200587m     Document Type: Article

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