Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue level

Biochemistry

Volumn 50, Issue 49, 2011, Pages 10567-10569

  McGlinchey, Ryan P ^a   Gruschus, James M ^a   Nagy, Attila ^a   Lee, Jennifer C ^a  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC PH; ELECTROSTATIC CHARGES; GLUTAMIC ACID; MELANIN SYNTHESIS; NEUTRAL PH; RESIDUE LEVEL;

AMINO ACIDS; ATOMIC FORCE MICROSCOPY; ATOMIC SPECTROSCOPY; DISSOLUTION; ELECTROSTATICS; MAGNETIC DOMAINS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

GLYCOPROTEINS;

AMYLOID; AMYLOID PME17; UNCLASSIFIED DRUG;

ARTICLE; ATOMIC FORCE MICROSCOPY; DISSOLUTION; FIBER; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PME17 REPEAT DOMAIN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN UNFOLDING; PROTON TRANSPORT; STATIC ELECTRICITY;

AMYLOID; GP100 MELANOMA ANTIGEN; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MICROSCOPY, ATOMIC FORCE; PROTEIN STRUCTURE, TERTIARY;

EID: 82955194492     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201578h     Document Type: Article

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