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. 1999 Nov;8(11):2251–2257. doi: 10.1110/ps.8.11.2251

Folding of an isolated ribonuclease H core fragment.

A K Chamberlain 1, K F Fischer 1, D Reardon 1, T M Handel 1, A S Marqusee 1
PMCID: PMC2144208  PMID: 10595528

Abstract

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.

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Selected References

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