How to remain nonfolded and pliable: The linkers in modular α-amylases as a case study

FEBS Journal

Volumn 278, Issue 13, 2011, Pages 2333-2340

  Feller, Georges ^a   Dehareng, Dominique ^a   Lage, Jean Luc Da ^b  

^a UNIVERSITY OF LIÈGE   (Belgium)

^b CNRS   (France)

Author keywords

amylases; glycoside hydrolases; intrinsically disordered proteins; protein folding; protein unfolding

Indexed keywords

AMYLASE; CYSTEINE; DISULFIDE; HYDROGEN; PROLINE; SERINE; THREONINE;

ARTICLE; CASE STUDY; CONTROLLED STUDY; DISULFIDE BOND; ENZYME CONFORMATION; ENZYME LOCALIZATION; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; RESIDUE ANALYSIS; SEQUENTIAL ANALYSIS;

ALPHA-AMYLASES; AMINO ACID SEQUENCE; ANIMALS; CAENORHABDITIS ELEGANS; CORBICULA; GLYCINE; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; MYTILUS EDULIS; PATELLA; PROLINE; PROTEIN CONFORMATION; PROTEIN FOLDING; PSEUDOALTEROMONAS;

EID: 80955178778     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08154.x     Document Type: Article

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