| Autor: |
Anna Katarina Tigerström |
| Rok vydání: |
2005 |
| Předmět: |
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| Zdroj: |
BIOS. 76:22-27 |
| ISSN: |
0005-3155 |
| DOI: |
10.1893/0005-3155(2005)076[0022:tbftop]2.0.co;2 |
| Popis: |
Adaptations of proteins towards an increased thermostability can be observed in nature in environments such as the marine hydrothermal vents. The principles behind an increased thermostability can then be used in the biotech industry in order to design proteins with high stability. The demand for an increased stability has to be balanced by the dynamic required for maintaining catalytic activity of the enzyme. The (hyper-)thermophilic proteins are composed of the common 20 natural amino acids. Optimization of interactions between the amino acids in the peptide chain is hence a key feature for an increased stability. By comparing structures of (hyper-)thermophilic proteins with the mesophilic counterparts it is demonstrated that an increased stability is achieved through a combination of a variety of stabilizing interactions. The thermostabilizing interactions include improved packing of the protein structure and optimization of hydrophobic and electrostatic interactions. Furthermore the structure... |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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