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Removal of surface charge-charge interactions from ubiquitin leaves the protein folded and very stable

The contribution of solvent-exposed charged residues to protein stability was evaluated using ubiquitin as a model protein. We combined site-directed mutagenesis and specific chemical modifications to first replace all Arg residues with Lys, followed by carbomylation of Lys-amino groups. Under the c...

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Hlavní autoři: Loladze, Vakhtang V., Makhatadze, George I.
Médium: Artigo
Jazyk:Inglês
Vydáno: Cold Spring Harbor Laboratory Press 2002
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2368776/
https://ncbi.nlm.nih.gov/pubmed/11742133
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