Why is Leu55→Pro55 transthyretin variant the most amyloidogenic: Insights from molecular dynamics simulations of transthyretin monomers

Protein Science

Volumn 12, Issue 6, 2003, Pages 1222-1231

  Yang, Mingfeng ^a   Lei, Ming ^a   Huo, Shuanghong ^a  

^a Carlson School of Chemistry and Biochemistry   (United States)

Author keywords

Amyloid deposit; Conformational change; Human transthyretin; Molecular dynamics simulation; Single point mutation

Indexed keywords

AMYLOID; LEUCINE; PREALBUMIN; PROLINE; RECOMBINANT PROTEIN; TRANSTHYRETIN RELATED AMYLOID FIBRIL PROTEIN, HUMAN; TRANSTHYRETIN-RELATED AMYLOID FIBRIL PROTEIN, HUMAN; AMYLOID PROTEIN; METHIONINE; MONOMER; MUTANT PROTEIN; VALINE;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; COMPUTER SIMULATION; GENETICS; HUMAN; HYDROGEN BOND; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; STRUCTURE ACTIVITY RELATION; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMYLOIDOSIS; BETA SHEET; COMPUTER PROGRAM; CONFORMATIONAL TRANSITION; MOLECULAR DYNAMICS; PRIORITY JOURNAL; SIMULATION; TIME;

AMYLOID; COMPUTER SIMULATION; HUMANS; HYDROGEN BONDING; LEUCINE; MODELS, MOLECULAR; POINT MUTATION; PREALBUMIN; PROLINE; PROTEIN CONFORMATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0037907526     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0239703     Document Type: Article

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