Structural highlights
Function
THM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis.
Publication Abstract from PubMed
A state-of-the-art review of the role of the Langmuir-Blodgett nanotemplate on protein crystal structures is here presented. Crystals grown by nanostructured template appear more radiation resistant than the classical ones, even in the presence of a third-generation highly focused beam at the European Synchrotron Radiation Facility. The electron density maps and the changes in parameters such as total diffractive power, B-factor, and pairwise R-factor have been discussed. Protein crystals, grown by the Langmuir-Blodgett nanotemplate-based method, proved to be more radiation resistant compared to crystals grown by the classical hanging drop method in terms of both global and specific damage.
Langmuir-blodgett nanotemplate and radiation resistance in protein crystals: state of the art.,Belmonte L, Pechkova E, Tripathi S, Scudieri D, Nicolini C Crit Rev Eukaryot Gene Expr. 2012;22(3):219-32. PMID:23140163[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Belmonte L, Pechkova E, Tripathi S, Scudieri D, Nicolini C. Langmuir-blodgett nanotemplate and radiation resistance in protein crystals: state of the art. Crit Rev Eukaryot Gene Expr. 2012;22(3):219-32. PMID:23140163
