Nuclear magnetic resonance studies of the denaturation of ubiquitin

Robert E. Lenkinski, Douglas M. Chen, Jerry D. Glickson, Gideon Goldstein

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Abstract

The effects of pH, temperature and guanidine hydrochloride concentration on the structure of ubiquitin, a polypeptide which can activate adenylate cyclase and can mimic thymopoietin induced differentiation of prothymocytes, were monitored using nuclear magnetic resonance spectroscopy. This relatively small polypeptide (molecular weight of 8541) exhibits a remarkable stability towards pH and temperature changes. At 7 M guanidine hydrochloride concentration, the structure of ubiquitin is essentially a random coil.

Original languageEnglish (US)
Pages (from-to)126-130
Number of pages5
JournalBBA - Protein Structure
Volume494
Issue number1
DOIs
StatePublished - Sep 27 1977

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ASJC Scopus subject areas

  • Medicine(all)

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Lenkinski, R. E., Chen, D. M., Glickson, J. D., & Goldstein, G. (1977). Nuclear magnetic resonance studies of the denaturation of ubiquitin. BBA - Protein Structure, 494(1), 126-130. https://doi.org/10.1016/0005-2795(77)90140-4