Nuclear magnetic resonance studies of the denaturation of ubiquitin

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

Research output: Contribution to journalArticle

63 Citations (Scopus)

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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Denaturation
Guanidine
Ubiquitin
Thymopoietins
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Peptides
Temperature
Adenylyl Cyclases
Nuclear magnetic resonance spectroscopy
Molecular Weight
Molecular weight

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Nuclear magnetic resonance studies of the denaturation of ubiquitin. / Lenkinski, Robert E.; Chen, Douglas M.; Glickson, Jerry D.; Goldstein, Gideon.

In: BBA - Protein Structure, Vol. 494, No. 1, 27.09.1977, p. 126-130.

Research output: Contribution to journalArticle

Lenkinski, Robert E. ; Chen, Douglas M. ; Glickson, Jerry D. ; Goldstein, Gideon. / Nuclear magnetic resonance studies of the denaturation of ubiquitin. In: BBA - Protein Structure. 1977 ; Vol. 494, No. 1. pp. 126-130.
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