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Probing the influence on folding behavior of structurally conserved core residues in P. aeruginosa apo-azurin
The effects on folding kinetics and equilibrium stability of core mutations in the apo-mutant C112S of azurin from Pseudomonas aeruginosa were studied. A number of conserved residues within the cupredoxin family were recognized by sequential alignment as constituting a common hydrophobic core: I7, F...
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| Autors principals: | , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
Cold Spring Harbor Laboratory Press
2004
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2286540/ https://ncbi.nlm.nih.gov/pubmed/15340166 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.04849004 |
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