Dedicated to the memory of R. Bruce Merrifield, Nobel Laureate, mentor and friend, and his family, role models all.
Back to the future: Ribonuclease A†
Article first published online: 14 SEP 2007
Copyright © 2008 Wiley Periodicals, Inc.
Special Issue: Special Issue Dedicated to the Memory of Bruce Merrifield
Volume 90, Issue 3, pages 259–277, 2008
How to Cite
Marshall, G. R., Feng, J. A. and Kuster, D. J. (2008), Back to the future: Ribonuclease A . Biopolymers, 90: 259–277. doi: 10.1002/bip.20845
- Issue published online: 21 APR 2008
- Article first published online: 14 SEP 2007
- Manuscript Accepted: 9 AUG 2007
- Manuscript Revised: 2 AUG 2007
- Manuscript Received: 27 APR 2007
- NIH. Grant Number: GM68460
- Computational Biology Training. Grant Number: GM 008802
- Division of Biology and Biomedical Science at Washington University in St. Louis, Ewing Marion Kauffman Foundation, Department of Biomedical Engineering at Washington University in St. Louis
- ribonuclease A;
- protein dynamics;
- chimeric enzyme
Pancreatic ribonuclease A (EC 126.96.36.199, RNase) is, perhaps, the best-studied enzyme of the 20th century. It was isolated by René Dubos, crystallized by Moses Kunitz, sequenced by Stanford Moore and William Stein, and synthesized in the laboratory of Bruce Merrifield, all at the Rockefeller Institute/University. It has proven to be an excellent model system for many different types of experiments, both as an enzyme and as a well-characterized protein for biophysical studies. Of major significance was the demonstration by Chris Anfinsen at NIH that the primary sequence of RNase encoded the three-dimensional structure of the enzyme. Many other prominent protein chemists/enzymologists have utilized RNase as a dominant theme in their research. In this review, the history of RNase and its offspring, RNase S (S-protein/S-peptide), will be considered, especially the work in the Merrifield group, as a preface to preliminary data and proposed experiments addressing topics of current interest. These include entropy–enthalpy compensation, entropy of ligand binding, the impact of protein modification on thermal stability, and the role of protein dynamics in enzyme action. In continuing to use RNase as a prototypical enzyme, we stand on the shoulders of the giants of protein chemistry to survey the future. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 90: 259–277, 2008.
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