Cold-Induced Changes in the Protein Ubiquitin

Conformational changes are essential for protein-protein and protein-ligand recognition. Here we probed changes in the structure of the protein ubiquitin at low temperatures in supercooled water using NMR spectroscopy. We demonstrate that ubiquitin is well folded down to 263 K, although slight rearr...

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Detalles Bibliográficos
Autores principales: Cho, Min-Kyu, Xiang, ShengQi, Kim, Hai-Young, Becker, Stefan, Zweckstetter, Markus
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3380907/
https://www.ncbi.nlm.nih.gov/pubmed/22737208
http://dx.doi.org/10.1371/journal.pone.0037270

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3380907/
https://www.ncbi.nlm.nih.gov/pubmed/22737208
http://dx.doi.org/10.1371/journal.pone.0037270

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