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A single disulfide bond restores thermodynamic and proteolytic stability to an extensively mutated protein.
The potential for engineering stable proteins with multiple amino acid substitutions was explored. Eleven lysine, five methionine, two tryptophan, one glycine, and three threonine substitutions were simultaneously made in barley chymotrypsin inhibitor-2 (CI-2) to substantially improve the essential...
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| Autori principali: | , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Cold Spring Harbor Laboratory Press
2000
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2144711/ https://ncbi.nlm.nih.gov/pubmed/11045611 |
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