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Structural Features in the Model of a Thermostable and Stress-resistant Protein, SP1 from aspen

Rathore, Ravindranath S and Narasimhamurthy, T (2004) Structural Features in the Model of a Thermostable and Stress-resistant Protein, SP1 from aspen. In: Journal of Biomolecular Structure and Dynamics, 21 (5). pp. 651-656.

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Abstract

A three dimensional theoretical model of SP1 (stable protein 1), which is resistant to high temperature and biotic-stresses, is presented here. The model was generated by the application of homology modeling technique. The conformational rigidity imparted to the fold by the presence of hydrogen-bonded, ${C_5}, {C_7}, {C_{10}}\hspace {5mm} and\hspace{5mm} {C_13}$ structures in the loop regions, multiple aromatic-aromatic interactions at the protein interior and on the surface, in addition to salt-links and hydrogen-bonds are primarily the major factors, responsible for the increased stability of protein. The putative protein family is characterized by motifs, E-x(0,1)-L-x-[AEGQS] and V-x(2,3)-L-x-[ADEGST] and the active site in the tertiary structure is formed by conserved aromatic and isoleucine clusters.

Item Type: Journal Article
Additional Information: The copyright of this article belongs to Adenine Press.
Keywords: Thermostability;Thermophilic;SP1;Aromatic clusters; Homology modeling
Department/Centre: Division of Physical & Mathematical Sciences > Physics
Date Deposited: 23 Jan 2006
Last Modified: 27 Aug 2008 11:41
URI: http://eprints.iisc.ernet.in/id/eprint/5168

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