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. 1977 Sep 27;494(1):126-30.
doi: 10.1016/0005-2795(77)90140-4.

Nuclear magnetic resonance studies of the denaturation of ubiquitin

R E Lenkinski, D M Chen, J D Glickson, G Goldstein

Nuclear magnetic resonance studies of the denaturation of ubiquitin

R E Lenkinski et al. Biochim Biophys Acta. .

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.

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