Amphiphilic α-helical potential: A putative folding motif adding few constraints to protein evolution

Journal of Molecular Evolution

Volumn 73, Issue 3-4, 2011, Pages 166-180

  Lee, S Y Ryan ^a   Parker, William ^a  

^a DUKE UNIVERSITY   (United States)

Author keywords

Amphiphilic; Evolution; Helical intermediate; Protein folding; Randomly occurring processes; Trifluoroethanol (TFE)

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; BACTERIAL PROTEIN; BETA 2 MICROGLOBULIN; INTERLEUKIN 6; PLASTOCYANIN; VEGETABLE PROTEIN;

ALGORITHM; AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; GENETICS; MOLECULAR EVOLUTION; MUTATION; NUCLEOTIDE SEQUENCE; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SALMONELLA TYPHI; SEQUENCE ANALYSIS; SPINACH; SWINE;

ALGORITHMS; AMINO ACID SEQUENCE; AMINO ACYL-TRNA SYNTHETASES; ANIMALS; BACTERIAL PROTEINS; BETA 2-MICROGLOBULIN; COMPUTER SIMULATION; CONSERVED SEQUENCE; EVOLUTION, MOLECULAR; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; INTERLEUKIN-6; MODELS, MOLECULAR; MUTATION; PLANT PROTEINS; PLASTOCYANIN; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SALMONELLA TYPHI; SEQUENCE ANALYSIS, PROTEIN; SPINACIA OLERACEA; SUS SCROFA;

EID: 84856343869     PISSN: 00222844     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00239-011-9465-0     Document Type: Article

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