Engineering more stable proteins
| Autor: | Romas J. Kazlauskas |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine Protein Denaturation Protein Folding Proteases Protein Conformation Protein Engineering Cleavage (embryo) 03 medical and health sciences Protein structure Side chain Animals Humans chemistry.chemical_classification Protein Stability Hydrogen bond Proteins General Chemistry Amino acid 030104 developmental biology Amino Acid Substitution chemistry biological sciences Biophysics Unfolded protein response Thermodynamics Protein folding |
| Zdroj: | Chemical Society Reviews. 47:9026-9045 |
| ISSN: | 1460-4744 0306-0012 |
| DOI: | 10.1039/c8cs00014j |
| Popis: | Protein function requires the folded protein form, but this form is unstable mainly because it readily unfolds into a flexible, unstructured form. Protein folding is favored by burying of hydrophobic side chains and hydrogen bonding between the amino acids. Protein unfolding is favored by the increase in conformational freedom of the main chain of amino acids upon unfolding. Protein stability is usually measured by the reversible unfolding of the protein with either heat or chemical additives like urea. Engineering mores stable proteins involves making substitutions that shift the folding-unfolding balance toward the folded form. Stabilizing substitutions can either stabilize the folded conformation or destabilize the unfolded ensemble. This tutorial emphasizes web-based tools to identify substitutions that stabilize proteins. Besides unfolding, other sources of protein instability are chemical modifications like oxidations or cleavage by proteases and aggregation of partly unfolded proteins into insoluble particles. |
| Databáze: | OpenAIRE |
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