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The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues
The periplasmic molecular chaperone protein SurA facilitates correct folding and maturation of outer membrane proteins in gram-negative bacteria. It preferentially binds peptides that have a high fraction of aromatic amino acids. Phage display selections, isothermal titration calorimetry and crystal...
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| Main Authors: | , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2007
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2040117/ https://ncbi.nlm.nih.gov/pubmed/17825319 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2007.07.069 |
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