Cargando…
Transient helicity in intrinsically disordered Axin-1 studied by NMR spectroscopy and molecular dynamics simulations
Many natural proteins are, as a whole or in part, intrinsically disordered. Frequently, such intrinsically disordered regions (IDRs) undergo a transition to a defined and often helical conformation upon binding to partner molecules. The intrinsic propensity of an IDR sequence to fold into a helical...
Autores principales: | Bomblies, Rainer, Luitz, Manuel Patrick, Scanu, Sandra, Madl, Tobias, Zacharias, Martin |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5371316/ https://www.ncbi.nlm.nih.gov/pubmed/28355271 http://dx.doi.org/10.1371/journal.pone.0174337 |
Ejemplares similares
-
Adenylylation of Tyr77 stabilizes Rab1b GTPase in an active state: A molecular dynamics simulation analysis
por: Luitz, Manuel P., et al.
Publicado: (2016) -
NMR characterization of solvent accessibility and transient structure in intrinsically disordered proteins
por: Hartlmüller, Christoph, et al.
Publicado: (2019) -
Covalent dye attachment influences the dynamics and conformational properties of flexible peptides
por: Luitz, Manuel P., et al.
Publicado: (2017) -
NMR spectroscopy enables simultaneous quantification of carbohydrates for diagnosis of intestinal and gastric permeability
por: Stryeck, Sarah, et al.
Publicado: (2018) -
Structural Characterization of Intrinsically Disordered Proteins by NMR Spectroscopy
por: Kosol, Simone, et al.
Publicado: (2013)