These authors contributed equally to this work.
Folding of an isolated ribonuclease H core fragment
Article first published online: 31 DEC 2008
Copyright © 1999 The Protein Society
Volume 8, Issue 11, pages 2251–2257, 1999
How to Cite
Chamberlain, A. K., Fischer, K. F., Reardon, D., Handel, T. M. and Marqusee, S. (1999), Folding of an isolated ribonuclease H core fragment. Protein Science, 8: 2251–2257. doi: 10.1110/ps.8.11.2251
- Issue published online: 31 DEC 2008
- Article first published online: 31 DEC 2008
- Manuscript Accepted: 16 JUL 1999
- Manuscript Received: 15 MAR 1999
- ribonuclease H;
- protein folding;
- protein fragments;
Based on results from both equilibrium and kinetic hydrogen exchange studies of Escherichia coli ribonuclease HI (RNase H), a fragment of RNase H (eABCD) was designed. The sequence of eABCD contains less than half of the protein's primary sequence and includes the regions that were shown to be the most protected from hydrogen exchange in all previous studies of RNase H. This core fragment of RNase H encodes a well-ordered protein with native-like properties. When isolated from the full-length monomeric protein, the eABCD fragment forms a stable dimer. However, we show indirectly that the monomeric form of eABCD is folded and has an overall secondary structure similar to the dimeric form.