Probing the surface of a sweet protein: NMR study of MNEI with a paramagnetic probe.
Ontology highlight
ABSTRACT: The design of safe sweeteners is very important for people who are affected by diabetes, hyperlipemia, and caries and other diseases that are linked to the consumption of sugars. Sweet proteins, which are found in several tropical plants, are many times sweeter than sucrose on a molar basis. A good understanding of their structure-function relationship can complement traditional SAR studies on small molecular weight sweeteners and thus help in the design of safe sweeteners. However, there is virtually no sequence homology and very little structural similarity among known sweet proteins. Studies on mutants of monellin, the best characterized of sweet proteins, proved not decisive in the localization of the main interaction points of monellin with its receptor. Accordingly, we resorted to an
SUBMITTER: Niccolai N
PROVIDER: S-EPMC2374096 | biostudies-literature | 2001 Aug
REPOSITORIES: biostudies-literature
ACCESS DATA