articleTop 10% cited
Staudinger Ligation: A Peptide from a Thioester and Azide
Organic Letters · 2000 · Vol. 2(13) · pp. 1939–1941
Bradley L. Nilsson✉(University of Wisconsin–Madison)Laura L. Kiessling(University of Wisconsin–Madison)Ronald T. Raines(University of Wisconsin–Madison)
Abstract
[reaction: see text] The technique of native chemical ligation enables the total chemical synthesis of proteins. This method is limited, however, by an absolute requirement for a cysteine residue at the ligation juncture. Here, this restriction is overcome with a new chemical ligation method in which a phosphinobenzenethiol is used to link a thioester and azide. The product is an amide with no residual atoms.
Chemical Synthesis and AnalysisMachine Learning in BioinformaticsBiochemical and Structural CharacterizationNative chemical ligationThioesterChemistryLigationChemical ligationAzideCysteineResidue (chemistry)AmideCombinatorial chemistry
MeSH terms
AzidesBiochemistryCysteineEstersPeptides
Funding
- National Institutes of Health
- Division of Chemistry
Citations
514
FWCI
2.93
field-weighted impact
References
14
Percentile
91%
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Citations per year
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