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Expressed Protein Ligation at Methionine: N-Terminal Attachment of Homocysteine, Ligation, and Masking

Tanaka, Tomohiro ; Wagner, Anne M. ; Warner, John B. ; Wang, Yanxin J. ; Petersson, E. James

Angewandte Chemie (International ed.), 2013-06, Vol.52 (24), p.6210-6213 [Periódico revisado por pares]

Weinheim: WILEY-VCH Verlag

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  • Título:
    Expressed Protein Ligation at Methionine: N-Terminal Attachment of Homocysteine, Ligation, and Masking
  • Autor: Tanaka, Tomohiro ; Wagner, Anne M. ; Warner, John B. ; Wang, Yanxin J. ; Petersson, E. James
  • Assuntos: Attachment ; chemoenzymatic reactions ; chemoselectivity ; Disengaging ; Enzymes ; Handles ; Homocysteine - chemistry ; ligation reactions ; Masking ; Methionine ; Methionine - chemistry ; protein synthesis ; Proteins ; Proteins - chemistry ; α-synuclein
  • É parte de: Angewandte Chemie (International ed.), 2013-06, Vol.52 (24), p.6210-6213
  • Notas: ArticleID:ANIE201302065
    Japan Society for the Promotion of Science (JSPS)
    istex:1267AAAA574790748B667D3FB1ACEA34178C1FDB
    ark:/67375/WNG-48R3JHMF-D
    University of Pennsylvania
    This work was supported by funding from the University of Pennsylvania and the Searle Scholars Program (10-SSP-214 to E.J.P.). T.T. was supported by a fellowship from the Japan Society for the Promotion of Science (JSPS). We thank Rakesh Kohli for assistance with HRMS (NIH RR-023444) and MALDI-MS (supported by NSF MRI-0820996).
    NIH - No. RR-023444
    Searle Scholars Program - No. 10-SSP-214
    NSF - No. MRI-0820996
    This work was supported by funding from the University of Pennsylvania and the Searle Scholars Program (10‐SSP‐214 to E.J.P.). T.T. was supported by a fellowship from the Japan Society for the Promotion of Science (JSPS). We thank Rakesh Kohli for assistance with HRMS (NIH RR‐023444) and MALDI‐MS (supported by NSF MRI‐0820996).
    ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
  • Descrição: A useful handle: One major limitation of protein semi‐synthesis is the need for Cys at the ligation site in native chemical ligation reactions. It is shown that a transferase enzyme can deliver homocysteine to the N‐terminus of an expressed protein (see scheme). Homocysteine can be used in a ligation reaction and then converted to Met. This allows one to use the MetArg or MetLys motif as a point of disconnection in semi‐synthesis.
  • Editor: Weinheim: WILEY-VCH Verlag
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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