Stability and folding of precursor and mature tryptophan-substituted ribose binding protein of Escherichia coli

A mutant ribose binding protein (REP) of Escherichia coli was obtained by site directed mutagenesis, replacing Phe-187 in the wild-type REP (WT-REP) with a Trp residue, in order to compare its stability and folding behavior with those of the WT-REP, The equilibrium unfolding properties and the folding kinetics of these proteins were monitored by fluorescence and circular dichroism (CD), For both WT-REP and the Trp-substituted REP (Trp-REP), the conformational stabilities of the precursor proteins and the mature proteins were the same, indicating that the signal peptide had no influence on the property of the mature domain, The Phe/Trp substitution in the mature domain, however, brought about a significant decrease in the conformational stability, The signal peptide had an appreciable retarding effect on the folding of the precursor Trp-REP as was reported for the WT-REP, Refolding kinetics of the WT-REP and Trp-REP showed a two-step reaction when monitored by fluorescence and by CD. (C) 1996 Academic Press, Inc.
Publisher
Elsevier Science Inc
Issue Date
1996
Language
ENG
Keywords

PHOSPHOGLYCERATE KINASE; SIGNAL SEQUENCE; PEPTIDES; RESIDUES

Citation

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, v.328, no.1, pp.78 - 84

ISSN
0003-9861
URI
http://hdl.handle.net/10203/73128
Appears in Collection
BS-Journal Papers(저널논문)
Files in This Item
There are no files associated with this item.
  • Hit : 129
  • Download : 0
  • Cited 0 times in thomson ci
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡClick to seewebofscience_button
⊙ Cited 7 items in WoSClick to see citing articles inrecords_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0