Examining Polyglutamine Peptide Length: A Connection between Collapsed Conformations and Increased Aggregation

Journal of Molecular Biology

Volumn 393, Issue 4, 2009, Pages 978-992

  Walters, Robert H ^a   Murphy, Regina M ^a  

^a University of Wisconsin Madison   (United States)

Author keywords

aggregation; dynamic light scattering; fluorescence resonance energy transfer (FRET); peptide conformation; polyglutamine

Indexed keywords

GLUTAMINE; PHOSPHATE BUFFERED SALINE; POLYGLUTAMINE;

ARTICLE; CONTROLLED STUDY; DILUTION; FLUORESCENCE RESONANCE ENERGY TRANSFER; LIGHT SCATTERING; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; PROTEIN SYNTHESIS; SEDIMENTATION; TRANSMISSION ELECTRON MICROSCOPY;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMANS; HUNTINGTON DISEASE; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; TRINUCLEOTIDE REPEAT EXPANSION;

EID: 70349838220     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.08.034     Document Type: Article

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