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Folding of an isolated ribonuclease H core fragment
Author(s) -
Chamberlain Aaron K.,
Fischer Kael F.,
Reardon Deirdre,
Handel Tracy M.,
Marqusee Susan
Publication year - 1999
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.8.11.2251
Subject(s) - rnase p , ribonuclease , dimer , rnase h , fragment (logic) , protein folding , folding (dsp implementation) , monomer , ribonuclease t1 , chemistry , sequence (biology) , s tag , stereochemistry , protein secondary structure , rnase mrp , crystallography , biochemistry , rna , gene , organic chemistry , computer science , electrical engineering , programming language , engineering , polymer
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.