At the molecular level, taste is one of the least understood sensory perceptions. A taste sensation is initiated by the interaction of a taste compound with taste receptors of taste buds on the tongue. One of the most studied tastes is sweetness. Sweet taste can be elicited to varying degrees by a wide variety of compounds such as mono- and di-saccharides, several amino acids, dipeptide derivatives such as aspartame, glycerol, cyclamates, saccharine, and some hydrated inorganic compounds. Comparison of the structures of these sweet compounds revealed no clues about what may be the chemical determinants of sweet taste. Furthermore, due to the low specificity of these compounds for the sweet receptors, it has been difficult to study the sweet taste sensory perception at the molecular level. Recent discovery of two unusual proteins, monellin and thaumatin, newly inspired the search for sweet determinants. These proteins are a few hundred thousand times sweeter than sugar on a molar basis and three to five thousand times sweeter on a weight basis. Such a high specificity makes these molecules the best system to study the interaction between the sweet receptor and its ligand. Our overall objective is to determine the 3-dimensional structures of monellin and thaumatin by x-ray crystallographic methods to lay a structural foundation for future studies on taste sensory perception at the molecular level.

Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Research Project (R01)
Project #
2R01NS015174-06A2
Application #
3396002
Study Section
Biophysics and Biophysical Chemistry A Study Section (BBCA)
Project Start
1979-01-01
Project End
1988-07-31
Budget Start
1985-08-01
Budget End
1986-07-31
Support Year
6
Fiscal Year
1985
Total Cost
Indirect Cost
Name
University of California Berkeley
Department
Type
Schools of Arts and Sciences
DUNS #
094878337
City
Berkeley
State
CA
Country
United States
Zip Code
94704
Glaeser, R M; Tong, L; Kim, S H (1989) Three-dimensional reconstructions from incomplete data: interpretability of density maps at ""atomic"" resolution. Ultramicroscopy 27:307-18
Kim, S H; Kang, C H; Kim, R et al. (1989) Redesigning a sweet protein: increased stability and renaturability. Protein Eng 2:571-5
Kang, C H; Kim, S H; Nikaido, K et al. (1989) Crystallization and preliminary X-ray studies of HisJ and LAO periplasmic proteins from Salmonella typhimurium. J Mol Biol 207:643-4
Jancarik, J; de Vos, A; Kim, S H et al. (1988) Crystallization of human c-H-ras oncogene products. J Mol Biol 200:205-7
Kim, S H; de Vos, A; Ogata, C (1988) Crystal structures of two intensely sweet proteins. Trends Biochem Sci 13:13-5
de Vos, A M; Hatada, M; van der Wel, H et al. (1985) Three-dimensional structure of thaumatin I, an intensely sweet protein. Proc Natl Acad Sci U S A 82:1406-9