Hostname: page-component-78c5997874-mlc7c Total loading time: 0 Render date: 2024-11-15T15:16:30.263Z Has data issue: false hasContentIssue false
  • English
  • Français

Folding of an isolated ribonuclease H core fragment

Published online by Cambridge University Press:  01 November 1999

AARON K. CHAMBERLAIN ,
KAEL F. FISCHER ,
DEIRDRE REARDON ,
TRACY M. HANDEL  and
SUSAN MARQUSEE
AARON K. CHAMBERLAIN
Affiliation:
Department of Molecular and Cell Biology, University of California, Berkeley, California 94720-3206
KAEL F. FISCHER
Affiliation:
Department of Molecular and Cell Biology, University of California, Berkeley, California 94720-3206
DEIRDRE REARDON
Affiliation:
Department of Molecular and Cell Biology, University of California, Berkeley, California 94720-3206
TRACY M. HANDEL
Affiliation:
Department of Molecular and Cell Biology, University of California, Berkeley, California 94720-3206
SUSAN MARQUSEE
Affiliation:
Department of Molecular and Cell Biology, University of California, Berkeley, California 94720-3206
Get access

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.

Keywords

ribonuclease Hprotein foldingprotein fragmentssubdomain
Type
Research Article
Information
Protein Science , Volume 8 , Issue 11 , November 1999 , pp. 2251 - 2257
Copyright
© 1999 The Protein Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)