Cargando…
Structure and Behavior of Human α-Thrombin upon Ligand Recognition: Thermodynamic and Molecular Dynamics Studies
Thrombin is a serine proteinase that plays a fundamental role in coagulation. In this study, we address the effects of ligand site recognition by alpha-thrombin on conformation and energetics in solution. Active site occupation induces large changes in secondary structure content in thrombin as show...
Autores principales: | Silva, Vivian de Almeira, Cargnelutti, Maria Thereza, Giesel, Guilherme M., Palmieri, Leonardo C., Monteiro, Robson Q., Verli, Hugo, Lima, Luis Mauricio T. R. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3173475/ https://www.ncbi.nlm.nih.gov/pubmed/21935446 http://dx.doi.org/10.1371/journal.pone.0024735 |
Ejemplares similares
-
Conformational Characterization of Ipomotaosides and Their Recognition by COX-1 and 2
por: Arantes, Pablo R., et al.
Publicado: (2014) -
Thrombin–aptamer recognition: a revealed ambiguity
por: Russo Krauss, Irene, et al.
Publicado: (2011) -
Identification and Mechanistic Analysis of a Novel Tick-Derived Inhibitor of Thrombin
por: Jablonka, Willy, et al.
Publicado: (2015) -
Large-scale molecular dynamics simulation: Effect of polarization on thrombin-ligand binding energy
por: Duan, Li L., et al.
Publicado: (2016) -
Thermodynamic, Anticoagulant, and Antiproliferative Properties of Thrombin Binding Aptamer Containing Novel UNA Derivative
por: Kotkowiak, Weronika, et al.
Publicado: (2017)