Cargando…
Time-dependent X-ray diffraction studies on urea/hen egg white lysozyme complexes reveal structural changes that indicate onset of denaturation
Temporal binding of urea to lysozyme was examined using X-ray diffraction of single crystals of urea/lysozyme complexes prepared by soaking native lysozyme crystals in solutions containing 9 M urea. Four different soak times of 2, 4, 7 and 10 hours were used. The five crystal structures (including t...
Autores principales: | Raskar, Tushar, Khavnekar, Sagar, Hosur, Madhusoodan |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5004150/ https://www.ncbi.nlm.nih.gov/pubmed/27573790 http://dx.doi.org/10.1038/srep32277 |
Ejemplares similares
-
High-pressure protein crystallography of hen egg-white lysozyme
por: Yamada, Hiroyuki, et al.
Publicado: (2015) -
Expression of Recombinant Human Lysozyme in Egg Whites of Transgenic Hens
por: Cao, Dainan, et al.
Publicado: (2015) -
Nanobeam precession-assisted 3D electron diffraction reveals a new polymorph of hen egg-white lysozyme
por: Lanza, Arianna, et al.
Publicado: (2019) -
The active site of hen egg-white lysozyme: flexibility and chemical bonding
por: Held, Jeanette, et al.
Publicado: (2014) -
New possibilities for egg white lysozyme: heat-denatured lysozyme partially inactivates select foot-and-mouth disease virus strains
por: Fukai, Katsuhiko, et al.
Publicado: (2021)