A carregar...

The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel

OmpA is one of only a few transmembrane proteins whose folding and stability have been investigated in detail. However, only half of the OmpA mass encodes its transmembrane β-barrel; the remaining sequence is a soluble domain that is localized to the periplasmic side of the outer membrane. To unders...

ver descrição completa

Na minha lista:
Detalhes bibliográficos
Main Authors: Danoff, Emily J., Fleming, Karen G.
Formato: Artigo
Idioma:Inglês
Publicado em: 2011
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3169180/
https://ncbi.nlm.nih.gov/pubmed/21782315
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpc.2011.06.013
Tags: Adicionar Tag
Sem tags, seja o primeiro a adicionar uma tag!