Abstract
The adaptation of native chemical ligation to protein semisynthesis has become a powerful way to address problems in the analysis of protein structure and function. In particular, the exploitation of nature's inteins in expressed protein ligation is now a standard approach in the study of proteins. Site-specific incorporation of unnatural amino acids, biophysical probes and post-translational modifications in proteins have led to new insights into enzyme mechanisms, protein folding, ion channel function, translation and signaling.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Amino Acids / chemistry
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Animals
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Arylalkylamine N-Acetyltransferase / chemistry
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Bacteriocins / biosynthesis
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Bacteriocins / chemistry
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Humans
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Peptide Fragments / chemistry
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Phosphorylation
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Potassium Channels / metabolism
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Protein Engineering / methods*
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Protein Prenylation
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Protein Processing, Post-Translational
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Proteins / chemical synthesis*
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Proteins / chemistry
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Proteins / genetics
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Proteins / metabolism
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Recombinant Proteins / chemical synthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Ribonuclease, Pancreatic / metabolism
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Ribonucleotide Reductases / chemistry
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Ribonucleotide Reductases / metabolism
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Zinc Fingers / genetics
Substances
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Amino Acids
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Bacteriocins
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Peptide Fragments
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Potassium Channels
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Proteins
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Recombinant Proteins
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Ribonucleotide Reductases
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Arylalkylamine N-Acetyltransferase
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Ribonuclease, Pancreatic