Structural highlights
Function
[MONA_DIOCU] Taste-modifying protein; intensely sweet-tasting protein. [MONB_DIOCU] Taste-modifying protein; intensely sweet-tasting protein.
Publication Abstract from PubMed
The racemic mixture of synthetic d and l-monellin has been crystallized, and its structure has been determined by X-ray crystallography at 1.9 A resolution. The crystal structure consists of two d and two l-monellin molecules in the P1 unit cell with a pseudo-centrosymmetrical arrangement. The final structure reveals small but significant structural differences between d and l-monellin in the same crystal. Possible reasons for these differences and their implications are discussed.
Structural differences in D and L-monellin in the crystals of racemic mixture.,Hung LW, Kohmura M, Ariyoshi Y, Kim SH J Mol Biol. 1999 Jan 8;285(1):311-21. PMID:9878408[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hung LW, Kohmura M, Ariyoshi Y, Kim SH. Structural differences in D and L-monellin in the crystals of racemic mixture. J Mol Biol. 1999 Jan 8;285(1):311-21. PMID:9878408 doi:S0022-2836(98)92308-7
