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Yi Liu

Researcher at Wuhan University

Publications -  703
Citations -  17777

Yi Liu is an academic researcher from Wuhan University. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 58, co-authored 537 publications receiving 14291 citations. Previous affiliations of Yi Liu include Hebei Medical University & Nanjing University of Aeronautics and Astronautics.

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Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin

TL;DR: The results of synchronous fluorescence spectra and UV-vis absorption spectra show that the conformation of bovine serum albumin has been changed, and the quenching mechanism of fluorescence of BSA by monoammonium glycyrrhizinate was discussed.
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Water-solubility of chitosan and its antimicrobial activity

TL;DR: In this paper, the antimicrobial mechanism of dissolved water-insoluble chitosan was hypothesized as forming an impervious layer around the cell, and the results suggest that optimum chitusan as food preservative should be water-incoverage from mild depolymerization.
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Studies of interaction between colchicine and bovine serum albumin by fluorescence quenching method

TL;DR: In this article, the interaction between colchicine and bovine serum albumin (BSA) was investigated by fluorescence and UV-Vis absorption spectroscopy, and the modified Stern-Volmer quenching constant K a and corresponding thermodynamic parameters Δ H, Δ G, Δ S at different temperatures were calculated.
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Investigation of the Interaction between Berberine and Human Serum Albumin

TL;DR: It was proved that the fluorescence quenching of HSA by berberine is a result of the formation of berberin-HSA complex and the results of thermodynamic parameters DeltaG, DeltaH, and DeltaS at different temperatures indicate that the electrostatic interactions play a major role for berberines- HSA association.
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Fluorescence Study on the Interaction of Bovine Serum Albumin with P-Aminoazobenzene

TL;DR: The synchronous fluorescence, CD and three-dimensional fluorescence spectral results showed that the hydrophobicity of amino acid residues increased and the losing of α-helix content in the presence of PAAB revealed that the microenvironment and conformation of BSA were changed in the binding reaction.