Cargando…
Smoothing a rugged protein folding landscape by sequence-based redesign
The rugged folding landscapes of functional proteins puts them at risk of misfolding and aggregation. Serine protease inhibitors, or serpins, are paradigms for this delicate balance between function and misfolding. Serpins exist in a metastable state that undergoes a major conformational change in o...
Autores principales: | Porebski, Benjamin T., Keleher, Shani, Hollins, Jeffrey J., Nickson, Adrian A., Marijanovic, Emilia M., Borg, Natalie A., Costa, Mauricio G. S., Pearce, Mary A., Dai, Weiwen, Zhu, Liguang, Irving, James A., Hoke, David E., Kass, Itamar, Whisstock, James C., Bottomley, Stephen P., Webb, Geoffrey I., McGowan, Sheena, Buckle, Ashley M. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5036219/ https://www.ncbi.nlm.nih.gov/pubmed/27667094 http://dx.doi.org/10.1038/srep33958 |
Ejemplares similares
-
Reactive centre loop dynamics and serpin specificity
por: Marijanovic, Emilia M., et al.
Publicado: (2019) -
Structural and dynamic properties that govern the stability of an engineered fibronectin type III domain
por: Porebski, Benjamin T., et al.
Publicado: (2015) -
Romanian Rugs
por: Petruscu, Paul
Publicado: (1966) -
Circumventing the stability-function trade-off in an engineered FN3 domain
por: Porebski, Benjamin T., et al.
Publicado: (2016) -
The Roles of Helix I and Strand 5A in the Folding, Function and Misfolding of α(1)-Antitrypsin
por: Knaupp, Anja S., et al.
Publicado: (2013)