Abstract:
:pMNEI, a single chain sweet protein related to monellin, has been studied by means of 1H NMR at 500 MHz. A partial sequential assignment performed by means of the MCD method allowed the determination of the secondary structure of a large portion of the beta-sheet of pMNEI that contains a likely 'sweet finger': the loop connecting the beta-strands from residue 59 to residue 78, corresponding to segment 16-35 of the A chain of monellin. The detailed three-dimensional structure of the loop (Tyr66-Ala67-Ser68-Asp69), determined from several interresidue and intraresidue NOEs and subsequent energy minimization, shows that the side chains of Tyr66 and Asp69 fit our model of the sweet receptor in a manner very similar to that of the side chains of Phe and Asp of aspartame.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Tancredi T,Iijima H,Saviano G,Amodeo P,Temussi PAdoi
10.1016/0014-5793(92)81138-ckeywords:
subject
Has Abstractpub_date
1992-09-21 00:00:00pages
27-30issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(92)81138-Cjournal_volume
310pub_type
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