D-RIBOSE STABILIZES PRECURSOR AND MATURE RIBOSE-BINDING PROTEINS OF ESCHERICHIA-COLI

Cited 1 time in webofscience Cited 0 time in scopus
  • Hit : 414
  • Download : 0
Heat- and guanidine hydrochloride-induced unfolding and refolding of precursor as well as mature ribose-binding proteins of Escherichia coli were studied in the presence of D-ribose using intrinsic tyrosine fluorescence and circular dichroism. The precursor and mature proteins have shown virtually identical unfolding-folding behavior. It was observed that D-ribose refolds partially unfolded precursor and mature ribose binding proteins into native structure and decreases the unfolding rate of the these proteins. The conformational stabilities of these proteins were found to increase with increasing D-ribose concentration.
Publisher
ELSEVIER SCIENCE BV
Issue Date
1994-02
Language
English
Article Type
Article
Keywords

INDUCED CONFORMATIONAL CHANGE; DENATURED PROTEINS; KINETIC ASPECTS; SUGAR BINDING; RECEPTOR; CHEMOTAXIS; TRANSPORT; LIGAND

Citation

FEBS LETTERS, v.339, no.1-2, pp.165 - 167

ISSN
0014-5793
DOI
10.1016/0014-5793(94)80407-9
URI
http://hdl.handle.net/10203/60826
Appears in Collection
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 1 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0