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
- Research Support, N.I.H., Extramural
- Research Support, Non-U.S. Gov't
- Review
MeSH terms
- Amino Acids / chemistry
- Animals
- Arylalkylamine N-Acetyltransferase / chemistry
- Bacteriocins / biosynthesis
- Bacteriocins / chemistry
- Humans
- Peptide Fragments / chemistry
- Phosphorylation
- Potassium Channels / metabolism
- Protein Engineering / methods*
- Protein Prenylation
- Protein Processing, Post-Translational
- Proteins / chemical synthesis*
- Proteins / chemistry
- Proteins / genetics
- Proteins / metabolism
- Recombinant Proteins / chemical synthesis
- Recombinant Proteins / chemistry
- Recombinant Proteins / genetics
- Ribonuclease, Pancreatic / metabolism
- Ribonucleotide Reductases / chemistry
- Ribonucleotide Reductases / metabolism
- Zinc Fingers / genetics
Substances
- Amino Acids
- Bacteriocins
- Peptide Fragments
- Potassium Channels
- Proteins
- Recombinant Proteins
- Ribonucleotide Reductases
- Arylalkylamine N-Acetyltransferase
- Ribonuclease, Pancreatic