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Nuclear Magnetic Resonance Structure of a Major Lens Protein, Human gamma C-Crystallin: Role of the Dipole Moment in Protein Solubility

Dixit, Karuna and Pande, Ajay and Pande, Jayanti and Sarma, Siddhartha P (2016) Nuclear Magnetic Resonance Structure of a Major Lens Protein, Human gamma C-Crystallin: Role of the Dipole Moment in Protein Solubility. In: BIOCHEMISTRY, 55 (22). pp. 3136-3149.

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Official URL: http://dx.doi.org/10.1021/acs.biochem.6b00359

Abstract

A hallmark of the crystallin proteins is their exceptionally high solubility, which is vital for maintaining the high refractive index of the eye lens. Human gamma C-crystallin is a major gamma-crystallin whose mutant forms are associated with congenital cataracts but whose three-dimensional structure is not known. An earlier study of a homology model concluded that human gamma C-crystallin has low intrinsic solubility, mainly because of the atypical magnitude and fluctuations of its dipole moment. On the contrary, the high-resolution tertiary structure of human gamma C-crystallin determined here shows unequivocally that it is a highly soluble, monomeric molecule in solution. Notable differences between the orientations and interactions of several side chains are observed upon comparison to those in the model. No evidence of the pivotal role ascribed to the effect of dipole moment on protein solubility was found. The nuclear magnetic resonance structure should facilitate a comprehensive understanding of the deleterious effects of cataract-associated mutations in human gamma C-crystallin.

Item Type: Journal Article
Additional Information: Copy right for this article belongs to the AMER CHEMICAL SOC, 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Depositing User: Id for Latest eprints
Date Deposited: 19 Jul 2016 09:55
Last Modified: 19 Jul 2016 09:55
URI: http://eprints.iisc.ac.in/id/eprint/54196

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