Fragment molecular orbital calculations reveal that the E200K mutation markedly alters local structural stability in the human prion protein

Prion

Volumn 4, Issue 1, 2010, Pages 38-44

  Hasegawa, Koji ^a   Mohri, Shirou ^b   Yokoyama, Takashi ^b  

^a ADVANCESOFT CORPORATION   (Japan)

^b NATIONAL INSTITUTE OF ANIMAL HEALTH   (Japan)

Author keywords

Creutzfeldt Jakob disease; Fragment molecular orbital calculation; Molecular interaction; Prion; Structural stability

Indexed keywords

PRION PROTEIN;

AB INITIO CALCULATION; AMINO ACID SUBSTITUTION; ARTICLE; CREUTZFELDT JAKOB DISEASE; HUMAN; MOLECULAR MODEL; POINT MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN VARIANT; AMINO ACID SEQUENCE; CHEMISTRY; GENETICS; MOLECULAR GENETICS; MUTATION; PRION; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; HUMANS; MOLECULAR SEQUENCE DATA; MUTATION; PRIONS; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY;

EID: 85046915826     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.4.1.10890     Document Type: Article

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