A thermodynamic approach to the conformational preferences of the 180-195 segment derived from the human prion protein α2-helix

Journal of Peptide Science

Volumn 15, Issue 1, 2009, Pages 30-35

  Ronga, Luisa ^a   Palladino, Pasquale ^a   Ragone, Raffaele ^a   Benedetti, Ettore ^a   Rossi, Filomena ^a  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

2 helix; sheet; Amyloid; CD titration; Prion protein; Prion toxicity; Structure inducing agents; Transmissible spongiform encephalopathies

Indexed keywords

ALANINE; PRION PROTEIN;

ALPHA HELIX; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS; THERMODYNAMICS; WILD TYPE;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PRIONS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS;

EID: 61749083187     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1086     Document Type: Article

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