Folding of the Ig-Like Domain of the Dengue Virus Envelope Protein Analyzed by High-Hydrostatic-Pressure NMR at a Residue-Level Resolution
Dengue fever is a mosquito-borne endemic disease in tropical and subtropical regions, causing a significant public health problem in Southeast Asia. Domain III (ED3) of the viral envelope protein contains the two dominant putative epitopes and part of the heparin sulfate receptor binding region that...
Main Authors: | Tomonori Saotome, Maxime Doret, Manjiri Kulkarni, Yin-Shan Yang, Philippe Barthe, Yutaka Kuroda, Christian Roumestand |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2019-07-01
|
Series: | Biomolecules |
Subjects: | |
Online Access: | https://www.mdpi.com/2218-273X/9/8/309 |
Similar Items
-
Comparative Assessment of NMR Probes for the Experimental Description of Protein Folding Pathways with High-Pressure NMR
by: Vincent Van Deuren, et al.
Published: (2021-07-01) -
Combining High-Pressure Perturbation with NMR Spectroscopy for a Structural and Dynamical Characterization of Protein Folding Pathways
by: Cécile Dubois, et al.
Published: (2020-11-01) -
Pressure and Chemical Unfolding of an α-Helical Bundle Protein: The GH2 Domain of the Protein Adaptor GIPC1
by: Cécile Dubois, et al.
Published: (2021-03-01) -
New approach to incorporating the impacts of non-hydrostatic perturbations in atmospheric models
by: Fa-Bo Zhang, et al.
Published: (2017-09-01) -
PERSPECTIVE HYDROSTATIC-MECHANICAL TRANSMISSIONS FOR WHEELED TRACTORS OF AGRICULTURAL SETTING
by: Samorodov, V., et al.
Published: (2013-01-01)