Sensitivity of secondary structure propensities to sequence differences between α- and γ-synuclein: Implications for fibrillation

Protein Science

Volumn 15, Issue 12, 2006, Pages 2795-2804

  Marsh, Joseph A ^a,b   Singh, Vinay K ^c   Jia, Zongchao ^c   Forman Kay, Julie D ^a,b  

^a HOSPITAL FOR SICK CHILDREN   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c QUEEN S UNIVERSITY   (Canada)

Author keywords

Chemical shift re referencing; NMR; Residual structure; Secondary chemical shifts; SNCG

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; GAMMA SYNUCLEIN;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; MATHEMATICAL COMPUTING; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SENSITIVITY ANALYSIS; STRUCTURE ANALYSIS;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; AMYLOID; ANIMALS; EVOLUTION, MOLECULAR; GAMMA-SYNUCLEIN; HUMANS; MAGNETIC RESONANCE IMAGING; MICE; MODELS, THEORETICAL; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 33751552347     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062465306     Document Type: Article

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