Cargando…
NMR Analysis of the Conformational Properties of the Trapped on-pathway Folding Intermediate of the Bacterial Immunity Protein Im7
Previous work shows that the transiently populated, on-pathway intermediate in Im7 folding contains three of the four native α-helices docked around a core stabilised by native and non-native interactions. To determine the structure and dynamic properties of this species in more detail, we have used...
Autores principales: | Whittaker, Sara B.-M., Spence, Graham R., Günter Grossmann, J., Radford, Sheena E., Moore, Geoffrey R. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2007
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2706327/ https://www.ncbi.nlm.nih.gov/pubmed/17188712 http://dx.doi.org/10.1016/j.jmb.2006.11.012 |
Ejemplares similares
-
Amino Acid Insertion Reveals a Necessary Three-Helical Intermediate in the Folding Pathway of the Colicin E7 Immunity Protein Im7
por: Knowling, Stuart E., et al.
Publicado: (2009) -
Single-Molecule Studies of the Im7 Folding Landscape
por: Pugh, Sara D., et al.
Publicado: (2010) -
Desolvation and Development of Specific Hydrophobic Core Packing during Im7 Folding
por: Bartlett, Alice I., et al.
Publicado: (2010) -
Folding versus aggregation: Polypeptide conformations on competing pathways
por: Jahn, Thomas R., et al.
Publicado: (2008) -
Intermediates: ubiquitous species on folding energy landscapes?
por: Brockwell, David J, et al.
Publicado: (2007)