Engineered metal-binding proteins: purification to protein folding
Autor: | Barry L. Haymore, Frances H. Arnold |
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Rok vydání: | 1991 |
Předmět: |
Models
Molecular Multidisciplinary Binding Sites Chemistry Protein Conformation Allosteric regulation food and beverages Cytochrome c Group Protein engineering Ligands Protein Engineering Combinatorial chemistry Folding (chemistry) Protein structure Biochemistry Membrane protein Metals Protein purification Protein folding Histidine Binding site Carrier Proteins |
Zdroj: | Science (New York, N.Y.). 252(5014) |
ISSN: | 0036-8075 |
Popis: | Proteins can make use of metal ions to bind substrates, to maintain structure, to effect catalysis, and for allosteric control and regulation. In order to hold a particular metal ion with high affinity and specificity, proteins form multidentate binding pockets designed to fulfill both the chemical and geometric bonding requirements of that metal. Metal recognition can be engineered into proteins for applications such as protein purification. |
Databáze: | OpenAIRE |
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