Consequences of proline-to-alanine substitutions for the stability and refolding of onconase

FEBS Journal

Volumn 280, Issue 18, 2013, Pages 4454-4462

  Hacke, Mandy ^a   Gruber, Tobias ^a   Schulenburg, Cindy ^a,b   Balbach, Jochen ^a   Arnold, Ulrich ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^b ETH ZURICH   (Switzerland)

Author keywords

onconase; proline isomerization; protein engineering; protein folding; thermodynamic stability

Indexed keywords

ALANINE; PROLINE; RANPIRNASE;

AMINO ACID SUBSTITUTION; ARTICLE; BIOPHYSICS; CATALYSIS; CHEMICAL ANALYSIS; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME RENATURATION; ENZYME STABILITY; FLUORESCENCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN REFOLDING; PROTEIN TERTIARY STRUCTURE; THERMODYNAMICS;

ONCONASE; PROLINE ISOMERIZATION; PROTEIN ENGINEERING; PROTEIN FOLDING; THERMODYNAMIC STABILITY;

ALANINE; AMINO ACID SUBSTITUTION; AMPHIBIAN PROTEINS; ANIMALS; BIOCATALYSIS; ESCHERICHIA COLI; KINETICS; MODELS, MOLECULAR; PROLINE; PROTEIN REFOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; RANA PIPIENS; RECOMBINANT PROTEINS; RIBONUCLEASES; THERMODYNAMICS;

RANA PIPIENS;

EID: 84883453181     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12406     Document Type: Article

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