Cargando…
Sequence Tolerance of a Single-Domain Antibody with a High Thermal Stability: Comparison of Computational and Experimental Fitness Profiles
[Image: see text] The sequence fitness of a llama single-domain antibody with an unusually high thermal stability is explored by a combined computational and experimental study. Starting with the X-ray crystallographic structure, RosettaBackrub simulations were applied to model sequence–structure to...
Autores principales: | Olson, Mark A., Legler, Patricia M., Zabetakis, Daniel, Turner, Kendrick B., Anderson, George P., Goldman, Ellen R. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2019
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6648363/ https://www.ncbi.nlm.nih.gov/pubmed/31460140 http://dx.doi.org/10.1021/acsomega.9b00730 |
Ejemplares similares
-
Evaluation of Disulfide Bond Position to Enhance the Thermal Stability of a Highly Stable Single Domain Antibody
por: Zabetakis, Dan, et al.
Publicado: (2014) -
Isolation and Epitope Mapping of Staphylococcal Enterotoxin B Single-Domain Antibodies
por: Turner, Kendrick B., et al.
Publicado: (2014) -
Contributions of the Complementarity Determining Regions to the Thermal Stability of a Single-Domain Antibody
por: Zabetakis, Dan, et al.
Publicado: (2013) -
Selection, characterization, and thermal stabilization of llama single domain antibodies towards Ebola virus glycoprotein
por: Liu, Jinny L., et al.
Publicado: (2017) -
Enhanced production of a single domain antibody with an engineered stabilizing extra disulfide bond
por: Liu, Jinny L., et al.
Publicado: (2015)