A synchrotron-based hydroxyl radical footprinting analysis of amyloid fibrils and prefibrillar intermediates with residue-specific resolution

Biochemistry

Volumn 53, Issue 49, 2014, Pages 7724-7734

  Klinger, Alexandra L ^a   Kiselar, Janna ^b   Ilchenko, Serguei ^b   Komatsu, Hiroaki ^a   Chance, Mark R ^b   Axelsen, Paul H ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CHAINS; MASS SPECTROMETRY; NEURODEGENERATIVE DISEASES; PEPTIDES; POLYPEPTIDES;

ALZHEIMER'S DISEASE; AMINO ACID RESIDUES; HYDROXYL RADICAL FOOTPRINTING; LINEAR POLYPEPTIDES; SOLID-STATE NUCLEAR MAGNETIC RESONANCE; SOLVENT ACCESSIBILITY; STRUCTURAL HETEROGENEITY; TOPOLOGICAL ARRANGEMENT;

GLYCOPROTEINS;

AMINO ACID; AMYLOID; AMYLOID BETA PROTEIN[1-40]; HYDROXYL RADICAL; SOLVENT; AMYLOID BETA PROTEIN; CROSS LINKING REAGENT; PEPSIN A; PEPTIDE FRAGMENT; RECOMBINANT PROTEIN;

ARTICLE; DARK FIELD ELECTRON MICROSCOPY; ELECTRON MICROSCOPY; MASS SPECTROMETRY; MEASUREMENT; NUCLEAR MAGNETIC RESONANCE; PROTEIN FOOTPRINTING; PROTEIN POLYMORPHISM; SOLID STATE; SYNCHROTRON; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; GENETICS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; METABOLISM; MOLECULAR WEIGHT; PEPTIDE MAPPING; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PULSE RADIOLYSIS; SURFACE PROPERTY; TANDEM MASS SPECTROMETRY; TRANSMISSION ELECTRON MICROSCOPY; ULTRASTRUCTURE;

AMYLOID; AMYLOID BETA-PEPTIDES; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CROSS-LINKING REAGENTS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HUMANS; HYDROXYL RADICAL; MICROSCOPY, ELECTRON, TRANSMISSION; MODELS, MOLECULAR; MOLECULAR WEIGHT; PEPSIN A; PEPTIDE FRAGMENTS; PEPTIDE MAPPING; PROTEIN CONFORMATION; PROTEOLYSIS; PULSE RADIOLYSIS; RECOMBINANT PROTEINS; SURFACE PROPERTIES; SYNCHROTRONS; TANDEM MASS SPECTROMETRY;

EID: 84918567048     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi5010409     Document Type: Article

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