Nuclear magnetic resonance studies of the denaturation of ubiquitin.
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.
D006146:Guanidines / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D009698:Nucleoproteins; D010455:Peptides; D011487:Protein Conformation; D011489:Protein Denaturation; D013696:Temperature
D006146:Guanidines; D009698:Nucleoproteins; D010455:Peptides