A side‐chain unprotected peptide with C‐terminal thioesters can chemoselectively react with another side‐chain unprotected peptide carrying an N‐terminal cysteine residue to afford the ligated peptide generating the Xaa‐Cys linkage at the co...
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https://www.riss.kr/link?id=O120662008
2018년
-
0947-6539
1521-3765
SCI;SCIE;SCOPUS
학술저널
n/a-n/a [※수록면이 p5 이하이면, Review, Columns, Editor's Note, Abstract 등일 경우가 있습니다.]
0
상세조회0
다운로드다국어 초록 (Multilingual Abstract)
A side‐chain unprotected peptide with C‐terminal thioesters can chemoselectively react with another side‐chain unprotected peptide carrying an N‐terminal cysteine residue to afford the ligated peptide generating the Xaa‐Cys linkage at the co...
A side‐chain unprotected peptide with C‐terminal thioesters can chemoselectively react with another side‐chain unprotected peptide carrying an N‐terminal cysteine residue to afford the ligated peptide generating the Xaa‐Cys linkage at the conjunction site (where Xaa is any amino acid). Advancements of chemoselective desulfurization methods have enabled converting the cysteine residue of the ligation product into alanine, thus expanding the repertoire of native chemical ligation. For a full discussion see the Concept article by K. Jin and X. Li on page 17397 ff.
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