Title :
Notice of Retraction
The Interaction between Rutin and Lysozyme
Author :
Ning-sheng Chen ; Li-li Sun ; Rui-ping Fang
Author_Institution :
Coll. of Biol. & Chem. Eng., Anhui Polytech. Univ., Wuhu, China
Abstract :
Notice of Retraction
After careful and considered review of the content of this paper by a duly constituted expert committee, this paper has been found to be in violation of IEEE´s Publication Principles.
We hereby retract the content of this paper. Reasonable effort should be made to remove all past references to this paper.
The presenting author of this paper has the option to appeal this decision by contacting TPII@ieee.org.
The interaction between Rutin and Lysozyme was studied using fluorescence, UV/vis, circular dichroism and FT-IR spectra. The fluorescence quenching mechanism was a static quenching procedure, the binding constants (KA) were 1.10×103 (298K) , 1.08×103 (303K) and 0.38×103 (308K) L-molι, the binding sites (n) were 1.52, 1.49, 1.34 respectively; Accroding to Ross´s theory, hydrophobic and Vander Waals force played a major role. The distance was 3.69 nm based on Forster non-radiative energy transfer theory. The results of Synchronous fluorescence, CD and FT-IR spectra indicated that the secondary structure of Lysozyme was changed .
Keywords :
Fourier transform spectra; biochemistry; circular dichroism; enzymes; fluorescence; infrared spectra; molecular biophysics; molecular configurations; radiation quenching; ultraviolet spectra; van der Waals forces; FTIR spectra; Forster nonradiative energy transfer theory; Ross theory; UV-vis spectra; binding constants; circular dichroism; fluorescence; fluorescence quenching; hydrophobic force; lysozyme; rutin; secondary structure; static quenching; van der Waals force; Chemicals; Compounds; Energy exchange; Fluorescence; Proteins; Spectroscopy;
Conference_Titel :
Bioinformatics and Biomedical Engineering, (iCBBE) 2011 5th International Conference on
Conference_Location :
Wuhan
Print_ISBN :
978-1-4244-5088-6
DOI :
10.1109/icbbe.2011.5780278
