A New Method for Estimating Protein Stability: the Work of Nick Pace
Year: 2008
Type: article
Abstract: Urea and Guanidine Hydrochloride Denaturation of Ribonuclease, Lysozyme, α-Chymotrypsin, and β-Lactoglobulin (Greene, R. F., Jr., and Pace, C. N. (1974) J. Biol. Chem. 249, 5388–5393) Carlos Nick Pace was born in Salt Lake City, Utah in 1940. He received his B.S. in chemistry from the University of Utah in 1962 and his Ph.D. in biochemistry from Duke University in 1966. For his Ph.D. research, Pace worked with Journal of Biological Chemistry (JBC) Classic author Charles Tanford (1JBC Classics Nozaki Y. Tanford C. J. Biol. Chem. 1970; 245: 1648-1652Abstract Full Text PDF PubMed Google ScholarNozaki Y. Tanford C. J. Biol. Chem. 1971; 246: 2211-2217http://www.jbc.org/cgi/content/full/283/4/e3Date: 2007Abstract Full Text PDF PubMed Google Scholar), who was interested in protein denaturation and solubility in various solutions. After doing a postdoctoral fellowship from 1966 to 1968 with Gordon Hammes at Cornell University, Pace joined the faculty of the Department of Biochemistry and Biophysics at Texas A&M University. As an independent researcher, Pace used the ideas and techniques he learned in Tanford's laboratory to study protein folding and denaturation. The JBC Classic reprinted here describes a new method for estimating protein stability called the linear extrapolation method. The method is the most widely used method for measuring protein stability, and the paper has been cited more than 370 times. In the paper, Pace and Raymond F. Greene, Jr. used optical rotation measurements to follow the unfolding of ribonuclease, lysozyme, α-chymotrypsin, and goat β-lactoglobulin in urea and guanidine hydrochloride. By analyzing the proteins' denaturation curves, they were able to make linear plots of the free energy of unfolding (ΔG) versus denaturant concentration. The plot's intercept gave a measure of the protein's stability whereas the slope gave an “m value” that measured how strongly ΔG depended on urea concentration. Pace's follow-up paper on m values (2Myers J.K. Pace C.N. Scholtz J.M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding..Protein Sci. 1995; 4: 2138-2148Crossref PubMed Scopus (1677) Google Scholar) is the third most cited paper in the history of Protein Science with about 800 citations. Today, Pace remains at Texas A&M where he is a distinguished professor at the Health Science Center. He has received many awards and honors for his contributions to science, including a Texas A&M University Association of Former Students Faculty Distinguished Achievement Award in Research (1999) and a Distinguished Achievement Award for Teaching (1990), a Texas A&M University System Health Science Center College of Medicine Senior Investigator Excellence in Research Award (1999), the Texas A&M University Regents Professor Service Award (2001), and the Sigma Xi Distinguished Scientist Award (2002).
Source: Journal of Biological Chemistry
Authors: Nicole Kresge, Robert D. Simoni, Robert L. Hil
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W2124667297