Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 81, Issue -, Pages 942-950Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2015.09.041
Keywords
Rice glutelin; Amylose; Hydrophobic interaction; Conformation; Molecular modeling
Funding
- National Natural Science Foundation of China [3171953]
- National Science and Technology Plan Projects [2012BAD37B02-02, 2012BAD34B0203]
Ask authors/readers for more resources
The interaction of rice glutelin (RG) with amylose was characterized by spectroscopic and molecular docking studies. The intrinsic fluorescence of RG increased upon the addition of amylose. The binding sites, binding constant and thermodynamic features indicated that binding process was spontaneous and the main driving force of the interaction was hydrophobic interaction. The surface hydrophobicity of RG decreased with increasing amount of amylose. Furthermore, synchronous fluorescence and circular dichroism (CD) spectra provided data concerning conformational and micro-environmental changes of RG. With the concentration of amylose increasing, the polarity around the tyrosine residues increased while the hydrophobicity decreased. Alteration of protein conformation was observed with increasing of a-helix and reducing of beta-sheet. Finally, a visual representation of two binding sites located in the amorphous area of RG was presented by molecular modeling studies. (C) 2015 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available