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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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Detalhes bibliográficos
Main Authors: Engman, K. Cecilia, Sandberg, Anders, Leckner, Johan, Karlsson, B. Göran
Formato: Artigo
Idioma:Inglês
Publicado em: Cold Spring Harbor Laboratory Press 2004
Assuntos:
Acesso em linha: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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