TY - JOUR
T1 - Nuclear magnetic resonance studies of the denaturation of ubiquitin
AU - Lenkinski, Robert E.
AU - Chen, Douglas M.
AU - Glickson, Jerry D.
AU - Goldstein, Gideon
N1 - Funding Information:
This work was supported by U.S. Public Health Service Grants CA-13148 (JDG), CA-08747 (GG), and Contract Grant CB-53868 (GG).
PY - 1977/9/27
Y1 - 1977/9/27
N2 - 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.
AB - 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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U2 - 10.1016/0005-2795(77)90140-4
DO - 10.1016/0005-2795(77)90140-4
M3 - Article
C2 - 20153
AN - SCOPUS:0017698893
SN - 0005-2795
VL - 494
SP - 126
EP - 130
JO - BBA - Protein Structure
JF - BBA - Protein Structure
IS - 1
ER -