TY - JOUR
T1 - Cold denaturation of CheY
AU - DeKoster, Gregory T.
AU - Robertson, Andrew D.
N1 - Funding Information:
The authors thank Dr K. P. Murphy for many helpful discussions and Drs Ann M. Stock and Jeffry B. Stock for supplying protein. This work was supported in part by grants from the University of Iowa Cancer Center, Eli Lilly & Co., and the NIH (GM 46869).
PY - 1995/6/9
Y1 - 1995/6/9
N2 - The thermal stability of the bacterial chemotaxis protein CheY from Salmonella typhimurium has been examined by thermal denaturation at pH 7.0 in the presence of guanidine-HCl and urea. For both denaturants, thermal denaturation monitored by circular dichroism spectropolarimetry consists of transitions both above and below 25°C, which is strong evidence for a heat capacity change that is ≥1500 cal/(mol K) upon unfolding. While many data for chemical and thermal denaturation are consistent with data for CheY from Escherichia coli, the observation of cold denaturation for S. typhimurium CheY is inconsistent with the small heat capacity change, 600 to 850 cal/(mol K), reported for denaturation of the E. coli protein.
AB - The thermal stability of the bacterial chemotaxis protein CheY from Salmonella typhimurium has been examined by thermal denaturation at pH 7.0 in the presence of guanidine-HCl and urea. For both denaturants, thermal denaturation monitored by circular dichroism spectropolarimetry consists of transitions both above and below 25°C, which is strong evidence for a heat capacity change that is ≥1500 cal/(mol K) upon unfolding. While many data for chemical and thermal denaturation are consistent with data for CheY from Escherichia coli, the observation of cold denaturation for S. typhimurium CheY is inconsistent with the small heat capacity change, 600 to 850 cal/(mol K), reported for denaturation of the E. coli protein.
KW - CheY
KW - Circular dichroism
KW - Denaturation
KW - Folding
UR - http://www.scopus.com/inward/record.url?scp=0029011161&partnerID=8YFLogxK
U2 - 10.1006/jmbi.1995.0315
DO - 10.1006/jmbi.1995.0315
M3 - Editorial
C2 - 7783208
AN - SCOPUS:0029011161
VL - 249
SP - 529
EP - 534
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 3
ER -