A tetrapeptide fragment-based design method results in highly stable artificial proteins

Proteins: Structure, Function and Genetics

Volumn 68, Issue 4, 2007, Pages 839-849

  Dallüge, Roman ^a   Oschmann, Jan ^a   Birkenmeier, Olaf ^a   Lücke, Christian ^b   Lilie, Hanke ^a   Rudolph, Rainer ^a   Lange, Christian ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^b MAX PLANCK RESEARCH UNIT FOR ENZYMOLOGY OF PROTEIN FOLDING   (Germany)

Author keywords

Artificial fold; Backbone conformation; Fragment based libraries; Protein design; Thermodynamic stability

Indexed keywords

POLYPEPTIDE; PROTEIN M5; PROTEIN M7; PSEUDOPEPTIDE; TETRAPEPTIDE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CIRCULAR DICHROISM; FLUORESCENCE SPECTROSCOPY; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TARGETING; TEMPERATURE;

AMINO ACID SEQUENCE; COMPUTER-AIDED DESIGN; COMPUTERS, MOLECULAR; INDICATORS AND REAGENTS; MAGNETIC RESONANCE SPECTROSCOPY; OLIGOPEPTIDES; PEPTIDE FRAGMENTS; PROTEINS; SPECTROMETRY, FLUORESCENCE; ULTRACENTRIFUGATION;

EID: 34548741301     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21493     Document Type: Article

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