Principal component analysis of alpha-helix deformations in transmembrane proteins.
α-helices are deformable secondary structural components regularly observed in protein folds. The overall flexibility of an α-helix can be resolved into constituent physical deformations such as bending in two orthogonal planes and twisting along the principal axis. We used Principal Component Analy...
Guardado en:
Autores principales: | Alexander Bevacqua, Sachit Bakshi, Yu Xia |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/75872cd3ffb7421492670feeca4d7639 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Plasticity of seven-transmembrane-helix receptor heteromers in human vascular smooth muscle cells.
por: Lauren J Albee, et al.
Publicado: (2021) -
Methionine sulfoxides on prion protein Helix-3 switch on the alpha-fold destabilization required for conversion.
por: Giorgio Colombo, et al.
Publicado: (2009) -
Integrin α1 has a long helix, extending from the transmembrane region to the cytoplasmic tail in detergent micelles.
por: Chaohua Lai, et al.
Publicado: (2013) -
Transport of lipophilic carboxylates is mediated by transmembrane helix 2 in multidrug transporter AcrB
por: Christine Oswald, et al.
Publicado: (2016) -
An efficient alpha helix model and simulation framework for stationary electrostatic interaction force estimation
por: Guy G. Butcher, et al.
Publicado: (2021)