Shape and Quaternary Structure of a-Globulin from Sesame (Sesamum indicum L.) Seed as Revealed by Small Angle X-ray Scattering and Quasi-elastic Light Scattering

Plietz, P . and Damaschun, S. G. and Zirwer, D. and Gast, K. and Schwenke, K. D. and Prakash, V. (1986) Shape and Quaternary Structure of a-Globulin from Sesame (Sesamum indicum L.) Seed as Revealed by Small Angle X-ray Scattering and Quasi-elastic Light Scattering. Journal of Biological Chemistry, 261 (27). pp. 12686-12691.

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Abstract

The a-globulin from sesame seed has a molar mass of 2.7 X lo6 g mol", determined by x-ray scattering, and (2.8 f 0.3) lo6 g mol", determined by quasi-elastic light scattering. The radius of gyration Rc amounts to (4.1 2 0.1) nm and (3.9 f 0.2) nm as determined by Guinier approximation and from the distribution func- tion I)(x), respectively. The molecule has a Stokes radius& of (5.4 20.15) nm and a maximum dimension L of (11 e L e 15) nm. The translational diffusion coefficient D&,, and the ratio of frictional coefficients f / f m i . amount to (3.95 2 0.12) X 10" om2 s" and 1.25, respectively. The quaternary structure of the protein molecule is approximated by a model consisting of six spherical subunits situated at the vertices of an octa- hedron having the symmetry 32.

Item Type:	Article
Uncontrolled Keywords:	alpha-Globulin Sesame storage protein x-ray scattering quasi-elastic light scattering
Subjects:	600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
Divisions:	Protein Chemistry and Technology
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	09 Jan 2008 06:18
Last Modified:	17 Oct 2018 07:03
URI:	http://ir.cftri.res.in/id/eprint/1620

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