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.
Full text not available from this repository. (Request a copy)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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