NMR studies on structure and dynamics of the monomeric derivative of BS-RNase: new insights for 3D domain swapping.
Three-dimensional domain swapping is a common phenomenon in pancreatic-like ribonucleases. In the aggregated state, these proteins acquire new biological functions, including selective cytotoxicity against tumour cells. RNase A is able to dislocate both N- and C-termini, but usually this process req...
Saved in:
Main Authors: | Roberta Spadaccini, Carmine Ercole, Maria A Gentile, Domenico Sanfelice, Rolf Boelens, Rainer Wechselberger, Gyula Batta, Andrea Bernini, Neri Niccolai, Delia Picone |
---|---|
Format: | article |
Language: | EN |
Published: |
Public Library of Science (PLoS)
2012
|
Subjects: | |
Online Access: | https://doaj.org/article/d88c0885ac7e46de8a51d8d34b4ea61c |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Double domain swapping in bovine seminal RNase: formation of distinct N- and C-swapped tetramers and multimers with increasing biological activities.
by: Giovanni Gotte, et al.
Published: (2012) -
Playing RNase P evolution: swapping the RNA catalyst for a protein reveals functional uniformity of highly divergent enzyme forms.
by: Christoph Weber, et al.
Published: (2014) -
Structural and functional analysis of the DEAF-1 and BS69 MYND domains.
by: Fatiha Kateb, et al.
Published: (2013) -
Evaluación de nitratos y bacterias coliformes en pozos de la cuenca alta del arroyo pantanoso (Bs. As.)
by: L. I. Picone, et al.
Published: (2003) -
Floquet-enhanced spin swaps
by: Haifeng Qiao, et al.
Published: (2021)