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Updated: Jul 6, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
Published on: November 3, 2011
Conformational studies suggest that the double stranded beta helix scaffold provides an optimal balance between
M Rajavel1, Neema N Kulkarni, B Gopal
1Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
Abstract:
Proteins with the double stranded beta-helix (DSBH, also known as cupin) fold perform a diverse range of functions. In this study, Bacillus subtilis quercetinase was used as a model system to understand the conformational determinants of functional diversity within the cupin fold. Controlled proteolysis experiments revealed that this enzyme is active, thermo-stable and maintains its quaternary arrangement even after substantial (ca 33 %) cleavage of the protein. The results presented in this manuscript thus show that the DSBH scaffold offers a novel balance between protein stability and function by locating the active site and substrate recognition features in the most stable region of the protein.
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