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- Liu, Chengmei, et al. Show all 7 Authors
- International journal of biological macromolecules 2015 v.81 pp. 942-950
- amylose; binding sites; circular dichroism spectroscopy; fluorescence; glutelins; hydrophobic bonding; hydrophobicity; molecular models; protein conformation; rice; thermodynamics; tyrosine
- ... 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 hydrophobicit ...