Cargando…
The flexibility and dynamics of protein disulfide isomerase
We have studied the mobility of the multidomain folding catalyst, protein disulfide isomerase (PDI), by a coarse‐graining approach based on flexibility. We analyze our simulations of yeast PDI (yPDI) using measures of backbone movement, relative positions and orientations of domains, and distances b...
Autores principales: | Römer, Rudolf A., Wells, Stephen A., Emilio Jimenez‐Roldan, J., Bhattacharyya, Moitrayee, Vishweshwara, Saraswathi, Freedman, Robert B. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5111589/ https://www.ncbi.nlm.nih.gov/pubmed/27616289 http://dx.doi.org/10.1002/prot.25159 |
Ejemplares similares
-
‘Something in the way she moves’: The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI)
por: Freedman, Robert B., et al.
Publicado: (2017) -
Protein disulfide isomerase in cardiovascular disease
por: Xiong, Bei, et al.
Publicado: (2020) -
Identification of protein disulfide isomerase 1 as a key isomerase for disulfide bond formation in apolipoprotein B100
por: Wang, Shiyu, et al.
Publicado: (2015) -
Functional Differences in Yeast Protein Disulfide Isomerases
por: Nørgaard, Per, et al.
Publicado: (2001) -
Protein Disulfide Isomerase and Host-Pathogen Interaction
por: Stolf, Beatriz S., et al.
Publicado: (2011)