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Conformational Studies Suggest That the Double Stranded \beta Helix Scaffold Provides an Optimal Balance Between Protein Stability and Function

Gopal, B and Rajavel, M and Kulkarni, Neema N (2008) Conformational Studies Suggest That the Double Stranded \beta Helix Scaffold Provides an Optimal Balance Between Protein Stability and Function. In: Protein and Peptide Letters, 15 (3). pp. 244-249.

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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.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Bentham Science.
Keywords: Double stranded beta helix;Cupin;Quercetinase;Conformational stability;Fragment complementation;Oligomerization.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 01 Apr 2008
Last Modified: 27 Aug 2008 13:18
URI: http://eprints.iisc.ernet.in/id/eprint/13620

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