Cargando…
Remarkable Rigidity of the Single α-Helical Domain of Myosin-VI As Revealed by NMR Spectroscopy
[Image: see text] Although the α-helix has long been recognized as an all-important element of secondary structure, it generally requires stabilization by tertiary interactions with other parts of a protein’s structure. Highly charged single α-helical (SAH) domains, consisting of a high percentage (...
Autores principales: | Barnes, C. Ashley, Shen, Yang, Ying, Jinfa, Takagi, Yasuharu, Torchia, Dennis A., Sellers, James R., Bax, Ad |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2019
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6556874/ https://www.ncbi.nlm.nih.gov/pubmed/31117653 http://dx.doi.org/10.1021/jacs.9b03116 |
Ejemplares similares
-
Imino Hydrogen Positions
in Nucleic Acids from Density
Functional Theory Validated by NMR Residual Dipolar Couplings
por: Grishaev, Alexander, et al.
Publicado: (2012) -
Long single α-helical tail domains bridge the gap between structure and function of myosin VI
por: Spink, Benjamin J, et al.
Publicado: (2008) -
NMR Observation of Sulfhydryl Signals in SARS‐CoV‐2 Main Protease Aids Structural Studies
por: Robertson, Angus J., et al.
Publicado: (2022) -
Dynamic Exchange of Myosin VI on Endocytic Structures
por: Bond, Lisa M., et al.
Publicado: (2012) -
Atomic resolution dynamics on the surface of amyloid β protofibrils probed by solution NMR
por: Fawzi, Nicolas L., et al.
Publicado: (2011)