Solid-phase synthesis and crystallization of monellin, an intensely sweet protein.
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چکیده
منابع مشابه
Solid-phase synthesis and crystallization of monellin, an intensely sweet protein.
Monellin, a sweet protein, consists of two noncovalently associated polypeptide chains, the A chain of 44 amino acid residues and the B chain of 50 residues. Two different primary structures have been reported for each of the A and B chains. The A and B chains corresponding to one of the reported monellin structures were synthesized by the stepwise solid-phase method using the Fmoc strategy in ...
متن کاملSolid-phase synthesis of crystalline [Ser41] B-chain monellin, an analogue of the sweet protein monellin.
The sweet protein monellin consists of two noncovalently associated polypeptide chains, the A chain of 44 amino acid residues and the B chain of 50 residues. Since blocking the free SH group of Cys41 in the B chain or treating the adjacent Met42 with CNBr removed its sweetness, this part of the molecule has been suggested to be essential for the sweetness. The [Ser41] B chain, an analogue of th...
متن کاملSolid-phase synthesis of crystalline monellin, a sweet protein.
The sweet protein, monellin, consists of two noncovalently associated polypeptide chains, the A chain of 44 amino acid residues and the B chain of 50 residues. The B chain was synthesized by the stepwise Fmoc solid-phase method in an overall yield of 6.2%. The synthetic B chain was combined with the synthetic A chain, which was left over from a previous work, to give monellin in a yield of 25.7...
متن کاملSolid-phase synthesis and crystallization of [Asn22, Gln25, Asn26]-A-chain-[Asn49, Glu50]-B-chain-monellin, an analogue of the sweet protein monellin.
The sweet protein monellin consists of two noncovalently associated polypeptide chains, the A chain of 44 amino acid residues and the B chain of 50 residues. The [Asn22, Gln25, Asn26]-A chain, an anologue of the A chain, was synthesized by the stepwise Fmoc-solid-phase method in an overall yield of 13.4%. The synthetic A chain analogue was combined with the [Asn49, Glu50]-B chain, which was lef...
متن کاملFolding and stability of sweet protein single-chain monellin. An insight to protein engineering.
Engineered single-chain monellin (SCM) proteins were constructed by recombinant technology without disrupting the topology and sweet activity of native protein. Data from 8-anilinonaphthalene-1-sulfonic acid fluorescence, size-exclusion chromatography, and heteronuclear NMR strongly suggest the presence of a folding intermediate at 1.5 m GdnHCl for SCM protein. The structural feature of the fol...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1990
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.54.1521