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Title:
Kinetic analysis of copper transfer from a chaperone to its target protein mediated by complex formation - Chemical Communications (RSC Publishing)
Description:
Chaperone proteins that traffic copper around the cell minimise its toxicity by maintaining it in a tightly bound form. The transfer of copper from chaperones to target proteins is promoted by complex formation, but the kinetic characteristics of transfer have yet to be demonstrated for any chaperone-target
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Keywords {π}
journals, books, article, copper, transfer, copz, databases, copaab, search, chaperone, complex, formation, chemistry, jump, site, publishing, kinetic, target, protein, kristine, liang, leonardo, justin, chloe, margaret, simone, nick, brun, author, proteins, rate, cui, dissociation, download, supplementary, information, open, access, permissions, cookies, main, content, advanced, issue, previous, journal, chemical, communications, analysis, mediated,
Topics {βοΈ}
chaperone-target protein pair atx1-type chaperone copz simone ciofi-baffonib target protein mediated 1039/c6cc08966f article type tightly bound form merck index marinlit related download options share search articles liang zhou leonardo tenori website collects cookies open access target proteins org journals chloe singleton books databases kinetic characteristics author kristine journals download citation search advanced 2017 previous article complex formationβ cell minimise complex formation report studies bacillus subtilis soluble domains occur rapidly magnitude higher data demonstrate dramatically enhances communication submitted user experience site search traffic copper publishing chaperone kay justin rate constant copper transfer kihlken nick bradley margaret //doi article
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