C. Nick Pace
Papers
1
Total Citations
2
H-Index
1
About
C. Nick Pace is best known for foundational contributions to protein folding and stability, a field in which his work has shaped modern biophysical chemistry. His research centers on the thermodynamics of protein denaturation, the role of disulfide bonds in stabilizing native structures, and the development of empirical scales for amino acid side-chain interactions. Pace’s landmark studies on ribonuclease A and other model proteins provided some of the first rigorous measurements of conformational stability, using urea and guanidine hydrochloride denaturation to quantify free energy changes. These contributions have been cited thousands of times, forming the empirical backbone for predicting protein folding pathways and engineering more stable proteins. Among his most notable achievements is the Pace hydrophobicity scale, which remains a standard reference for estimating the contribution of nonpolar residues to protein stability. His work has also advanced understanding of the pH dependence of stability and the energetic penalties of introducing charged residues into protein cores. For students and researchers, Pace’s papers are essential reading for anyone seeking to grasp the quantitative principles underlying protein folding and design.
Research Focus
Key Achievements
Top Papers
- 1