Unnatural Amino Acid Mutagenesis: A Precise Tool for Probing Protein Structure and Function
| Autor: | Pamela M. England |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
chemistry.chemical_classification
Protein structure and function General method Molecular Structure Protein Conformation Proteins Mutagenesis (molecular biology technique) Translation (biology) DNA Biology Biochemistry Transmembrane protein Amino acid Protein structure RNA Transfer chemistry Codon Nonsense Mutagenesis Protein Biosynthesis Protein biosynthesis Animals Amino Acids |
| Zdroj: | Biochemistry. 43:11623-11629 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi048862q |
| Popis: | The first general method for the biosynthetic incorporation of unnatural amino acids into proteins was reported in 1989. The ensuing years have seen the solid development and subsequent implementation of "unnatural amino acid mutagenesis" in a number of groundbreaking studies. Over 100 different amino acids have been incorporated into dozens of soluble and transmembrane proteins, using both cell-extract and cell-intact translation systems. The approach has provided insights into ligand-binding sites, conformational changes, and protein-protein interactions with a level of precision simply unparalleled by conventional mutagenesis. Here, the methodology is outlined, significant applications of the approach are summarized, and recent major improvements in the method are discussed. The future will likely see many more investigators utilizing this approach to manipulate proteins as it realizes its promise of becoming a tool with enormous potential. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|