Cargando…
Temperature dependence of NMR chemical shifts: Tracking and statistical analysis
Isotropic chemical shifts measured by solution nuclear magnetic resonance (NMR) spectroscopy offer extensive insights into protein structure and dynamics. Temperature dependences add a valuable dimension; notably, the temperature dependences of amide proton chemical shifts are valuable probes of hyd...
Autores principales: | Trainor, Kyle, Palumbo, Jeffrey A., MacKenzie, Duncan W. S., Meiering, Elizabeth M. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley & Sons, Inc.
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6933856/ https://www.ncbi.nlm.nih.gov/pubmed/31730280 http://dx.doi.org/10.1002/pro.3785 |
Ejemplares similares
-
The BioGRID database: A comprehensive biomedical resource of curated protein, genetic, and chemical interactions
por: Oughtred, Rose, et al.
Publicado: (2020) -
PyXlinkViewer: A flexible tool for visualization of protein chemical crosslinking data within the PyMOL molecular graphics system
por: Schiffrin, Bob, et al.
Publicado: (2020) -
A backbone‐dependent rotamer library with high (ϕ, ψ) coverage using metadynamics simulations
por: Mortensen, Jennifer C., et al.
Publicado: (2022) -
Temperature Dependence of the Rotation and Hydrolysis Activities of F(1)-ATPase
por: Furuike, Shou, et al.
Publicado: (2008) -
The Dundee Resource for Sequence Analysis and Structure Prediction
por: MacGowan, Stuart A., et al.
Publicado: (2019)