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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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Main Authors: | , , , , |
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Formato: | Artigo |
Idioma: | Inglês |
Publicado em: |
Public Library of Science (PLoS)
2012-01-01
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Colecção: | PLoS ONE |
Acesso em linha: | http://europepmc.org/articles/PMC3380907?pdf=render |
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