Towards meeting the Paracelsus Challenge: The design, synthesis, and characterization of paracelsin-43, an α-helical protein with over 50% sequence identity to an all-β protein

Proteins: Structure, Function and Genetics

Volumn 24, Issue 4, 1996, Pages 502-513

  Jones, David T ^a,d   Moody, Claire M ^b   Uppenbrink, Julia ^a   Viles, John H ^c   Doyle, Paul M ^b   Harris, C John ^b   Pearl, Laurence H ^a   Sadler, Peter J ^c   Thornton, Janet M ^a  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

^b WELLCOME RESEARCH LABORATORIES   (United Kingdom)

^c UNIVERSITY OF LONDON   (United Kingdom)

^d UNIVERSITY OF WARWICK   (United Kingdom)

Author keywords

1H NMR; CD; de novo design; ethylene glycol; genetic algorithms; inverse folding; methanol; peptide; protein folding; protein structure

Indexed keywords

ETHYLENE GLYCOL; METHANOL;

ALGORITHM; ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; CIRCULAR DICHROISM; DRUG DESIGN; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN STRUCTURE;

ALGORITHMS; AMINO ACID SEQUENCE; ANTIMICROBIAL CATIONIC PEPTIDES; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0029881326     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199604)24:4<502::AID-PROT9>3.0.CO;2-F     Document Type: Article

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