Proceedings of the Korean Biophysical Society Conference (한국생물물리학회:학술대회논문집)
- 1999.06a
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- Pages.18-18
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- 1999
From Folding to Sweet Taste: NMR, Circular Dichroism and Fluorescence Studies on Sweet Protein, Monellin
- Lee, Weontae (Department of Biochemistry, College of Science, Yonsei University) ;
- Sung, Yoon-hui (Department of Biochemistry, College of Science, Yonsei University) ;
- Heedouk Hong (Department of Biochemistry, College of Science, Yonsei University) ;
- Chaejoon Cheong (Korea Basic Science Institut) ;
- Cho, Joong-Myung (Biotech Research Institute, LG Chem., Research Park)
- Published : 1999.06.01
Abstract
A sweet protein monellin was originally isolated from the berries of the West African plant Dioscoreophyllum cumminsii. The studies for molecular interaction of different sweeteners with receptor as well as receptor binding model have been proposed previously. The high-resolution solution structure of single-chain monellin (SCM) has been determined to investigate structural origin of sweet taste by NMR spectroscopy and simulated annealing calculations.(omitted)
Keywords