A preformed binding interface in the unbound ensemble of an intrinsically disordered protein: evidence from molecular simulations.
Intrinsically disordered proteins play an important role in cellular signalling, mediated by their interactions with other biomolecules. A key question concerns the nature of their binding mechanism, and whether the bound structure is induced only by proximity to the binding partner. This is difficu...
Saved in:
| Main Authors: | Michael Knott, Robert B Best |
|---|---|
| Format: | article |
| Language: | EN |
| Published: |
Public Library of Science (PLoS)
2012
|
| Subjects: | |
| Online Access: | https://doaj.org/article/fd65d11f517f41d3857c0a90b0c1415a |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Full structural ensembles of intrinsically disordered proteins from unbiased molecular dynamics simulations
by: Utsab R. Shrestha, et al.
Published: (2021) -
Incorporation of heparin-binding proteins into preformed dextran sulfate-chitosan nanoparticles
by: Zaman P, et al.
Published: (2016) -
Jerusalem Unbound
by: Muhammad Yaseen Gada
Published: (2015) -
Identification of ligand binding sites in intrinsically disordered proteins with a differential binding score
by: Qiao-Hong Chen, et al.
Published: (2021) -
Unbound Harvard journal of the legal left.
Published: (2005)