1. Protein-Templated Peptide Ligation**
- Author
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Nicolas Brauckhoff, Johannes T. H. Yeh, Tom N. Grossmann, Gernot Hahne, and AIMMS
- Subjects
Magnetic Resonance Spectroscopy ,Lysis ,Protein Conformation ,Peptide ,Catalysis ,protein modification ,Humans ,HSP70 Heat-Shock Proteins ,Protein Interaction Domains and Motifs ,bioorthogonal reactions ,chemistry.chemical_classification ,templated reactions ,Molecular Structure ,Chemistry ,General Chemistry ,Highly selective ,CREB-Binding Protein ,Combinatorial chemistry ,Peptide Fragments ,Orders of magnitude (mass) ,Template ,peptide ligation ,solid-phase peptide synthesis ,Nucleic acid ,Chemical ligation ,Ligation ,Myeloid-Lymphoid Leukemia Protein - Abstract
Molecular templates bind particular reactants, thereby increasing their effective concentrations and accelerating the corresponding reaction. This concept has been successfully applied to a number of chemical problems with a strong focus on nucleic acid templated reactions. We present the first protein-templated reaction that allows N-terminal linkage of two peptides. In the presence of a protein template, ligation reactions were accelerated by more than three orders of magnitude. The templated reaction is highly selective and proved its robustness in a protein-labeling reaction that was performed in crude cell lysate.
- Published
- 2014
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