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How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
Published on: February 11, 2019
Stability, catalytic versatility and evolution of the (beta alpha)(8)-barrel fold
B Höcker1, C Jürgens, M Wilmanns
1Universität zu Köln, Institut für Biochemie, Otto-Fischer-Strasse 12-14, D-50674 Köln, Germany.
Abstract:
The (beta alpha)(8)-barrel is a versatile single-domain protein fold that is adopted by a large number of enzymes. The (beta alpha)(8)-barrel fold has been used as a model to elucidate the structural basis of protein thermostability and in studies to interconvert catalytic activities or substrate specificities by rational design or directed evolution. Recently, the (beta alpha)(4)-half-barrel was identified as a possible structural subdomain.
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