Insufficient hydrogen-bond desolvation and prion-related disease

European Journal of Biochemistry

Volumn 269, Issue 17, 2002, Pages 4165-4168

  Fernández, Ariel ^a,b  

^a UNIVERSITY OF CHICAGO   (United States)

^b UNIVERSIDAD NACIONAL DEL SUR   (Argentina)

Author keywords

All atom trajectory; Backbone desolvation; Hydrogen bond; Prions; Protein folding

Indexed keywords

CELL PROTEIN; PRION PROTEIN; PROTEIN X; SOLVENT;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; HYDROGEN BOND; HYDROPHOBICITY; NONHUMAN; PATHOGENESIS; PHYSICAL CHEMISTRY; PRION DISEASE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STRUCTURE; SCRAPIE; SOLVATION;

ANIMALS; CRICETINAE; HUMANS; HYDROGEN BONDING; MESOCRICETUS; PRION DISEASES; PROTEIN CONFORMATION; PROTEIN FOLDING; PRPC PROTEINS; PRPSC PROTEINS; SOLUBILITY;

ANIMALIA;

EID: 0036049651     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03116.x     Document Type: Article

References (8)

1. Time-resolved backbone desolvation and mutational hot spots in folding proteins
2. Physical reasons for the unusual alpha-helical stabilization afforded by charged or neutral polar residues in alanine-rich peptides
3. Energetics of protein structure
4. Protein folding: Making a network of hydrophobic clusters
5. D/H amide kinetic isotopic effects reveal when hydrogen bonds form during protein folding
6. Pathways to a protein folding intermediate observed in a 1μs simulation in aqueous solution
7. Prions
8. NMR solution structure of the human prion protein