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Removal of surface charge-charge interactions from ubiquitin leaves the protein folded and very stable
The contribution of solvent-exposed charged residues to protein stability was evaluated using ubiquitin as a model protein. We combined site-directed mutagenesis and specific chemical modifications to first replace all Arg residues with Lys, followed by carbomylation of Lys-amino groups. Under the c...
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| Huvudupphovsmän: | , |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
Cold Spring Harbor Laboratory Press
2002
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2368776/ https://ncbi.nlm.nih.gov/pubmed/11742133 |
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