The human prion protein α2 helix: A thermodynamic study of its conformational preferences

Proteins: Structure, Function and Genetics

Volumn 59, Issue 1, 2005, Pages 72-79

  Tizzano, Barbara ^a   Palladino, Pasquale ^a   De Capua, Antonia ^a   Marasco, Daniela ^b   Rossi, Filomena ^a,c   Benedetti, Ettore ^a,c   Pedone, Carlo ^b   Ragone, Raffaele ^d   Ruvo, Menotti ^b,d,e  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b CNR   (Italy)

^c CIRPEB   (Italy)

^d SECOND UNIVERSITY OF NAPLES   (Italy)

^e CNR   (Italy)

Author keywords

helix; sheet; Circular dichroism; Conformational ambivalence; Spongiform encephalopathy; Structuring agents

Indexed keywords

ASPARAGINYLASPARAGINYLPHENYLALANYLVALYLHISTIDYLASPARTYLCYSTEINYLVALYLASPARAGINYLISOLEUCYLTHREONYLISOLEUCYLLYSYLGLUTAMINYLHISTIDYLTHREONYLVALYLTHREONYLTHREONYLTHREONYLTHREONYLLYSYLGLYCINE; DODECYL SULFATE SODIUM; PEPTIDE; PRION PROTEIN; TRIFLUOROETHANOL; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; HUMAN; MATHEMATICAL ANALYSIS; PREDICTION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; SYNTHESIS; TEMPERATURE; THERMODYNAMICS;

HUMANS; PRIONS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SODIUM DODECYL SULFATE; THERMODYNAMICS;

EID: 14644414777     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20395     Document Type: Article

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