Wild type and mutants of the HET-s(218-289) prion show different flexibility at fibrillar ends: A simulation study

Proteins: Structure, Function and Bioinformatics

Volumn 82, Issue 3, 2014, Pages 399-404

  Friedman, Ran ^a,b   Caflisch, Amedeo ^b  

^a LINNAEUS UNIVERSITY   (Sweden)

^b UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

Aggregation; Amyloid; Fibril growth; Molecular dynamics

Indexed keywords

AMYLOID; FUNGAL PROTEIN; HET S (218-289) AMYLOID FIBRIL; PHENYLALANINE; PRION PROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; FUNGUS MUTANT; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; SOLID STATE; WILD TYPE;

FUNGI; SOLENOIDEA;

AGGREGATION; AMYLOID; FIBRIL GROWTH; MOLECULAR DYNAMICS;

FUNGAL PROTEINS; MOLECULAR DYNAMICS SIMULATION; MUTATION; PLIABILITY; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION;

EID: 84893724428     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24402     Document Type: Article

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