Matches in SemOpenAlex for { <https://semopenalex.org/work/W1973680826> ?p ?o ?g. }
Showing items 1 to 87 of
87
with 100 items per page.
- W1973680826 endingPage "196" @default.
- W1973680826 startingPage "188" @default.
- W1973680826 abstract "UDP-galactose 4-epimerase from Escherichia coli is a homodimer of molecular weight 39 kDa/subunit having noncovalently bound NAD acting as cofactor. Denaturation by 8 M urea at pH 7.0 causes 85% loss of its secondary structure and dissociation of its constituent molecules. Dilution of the denaturant by buffer at pH 8.5 leads to functional reconstitution of the dimeric holoenzyme. The refolding process is biphasic: after 2 min an equilibrium conformer is formed having 72% of its native secondary structure and by 60 min reactivation becomes complete. The early intermediate has lower energy of activation against thermal denaturation than the reactivated state. Patterns of trypsin digestion suggests a native like structure of this intermediate. Variation of solvent viscosity and ionic strength and inclusion of proline cis-trans isomerase in the refolding process do not alter kinetics of reactivation. Moreover, unaltered kinetics of reactivation against variation of temperature, pH, and duration of denaturation strongly suggests absence of proline cis/trans isomerization. Measurement of kinetics of (i) recovery of tertiary structure by protein fluorescence; (ii) incorporation of NAD from quantitation of bound cofactor; (iii) formation of substrate binding site by specific interaction with extrinsic fluorophore 1-anilino-8-naphthalene sulfonic acid and quenching by 5'-UMP, a competitive inhibitor; and (iv) recovery of activity indicate that they are all comparable. It appears that internal rearrangement of the protein during refolding, shielded from solvent, is the rate-limiting step of generation of cofactor binding site which ultimately leads to maturation of the holoenzyme structure." @default.
- W1973680826 created "2016-06-24" @default.
- W1973680826 creator A5009765380 @default.
- W1973680826 creator A5049112022 @default.
- W1973680826 date "2001-07-01" @default.
- W1973680826 modified "2023-09-26" @default.
- W1973680826 title "UDP-Galactose 4-Epimerase from Escherichia coli: Formation of Catalytic Site during Reversible Folding" @default.
- W1973680826 cites W1479717924 @default.
- W1973680826 cites W1562907760 @default.
- W1973680826 cites W1608807138 @default.
- W1973680826 cites W1891017166 @default.
- W1973680826 cites W1966146291 @default.
- W1973680826 cites W1977025415 @default.
- W1973680826 cites W1980495958 @default.
- W1973680826 cites W1980694228 @default.
- W1973680826 cites W1984610175 @default.
- W1973680826 cites W1987845094 @default.
- W1973680826 cites W1992303218 @default.
- W1973680826 cites W1998274428 @default.
- W1973680826 cites W2017639307 @default.
- W1973680826 cites W2026300833 @default.
- W1973680826 cites W2035177298 @default.
- W1973680826 cites W2045589999 @default.
- W1973680826 cites W2047298861 @default.
- W1973680826 cites W2058340251 @default.
- W1973680826 cites W2072738087 @default.
- W1973680826 cites W2092496555 @default.
- W1973680826 cites W2095301078 @default.
- W1973680826 cites W2122845637 @default.
- W1973680826 cites W2156396050 @default.
- W1973680826 cites W2199874637 @default.
- W1973680826 cites W2205612390 @default.
- W1973680826 cites W2435401553 @default.
- W1973680826 cites W4211003552 @default.
- W1973680826 cites W4247739057 @default.
- W1973680826 doi "https://doi.org/10.1006/abbi.2001.2380" @default.
- W1973680826 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11437350" @default.
- W1973680826 hasPublicationYear "2001" @default.
- W1973680826 type Work @default.
- W1973680826 sameAs 1973680826 @default.
- W1973680826 citedByCount "4" @default.
- W1973680826 countsByYear W19736808262013 @default.
- W1973680826 crossrefType "journal-article" @default.
- W1973680826 hasAuthorship W1973680826A5009765380 @default.
- W1973680826 hasAuthorship W1973680826A5049112022 @default.
- W1973680826 hasConcept C121332964 @default.
- W1973680826 hasConcept C13965031 @default.
- W1973680826 hasConcept C148898269 @default.
- W1973680826 hasConcept C185592680 @default.
- W1973680826 hasConcept C204328495 @default.
- W1973680826 hasConcept C2776923230 @default.
- W1973680826 hasConcept C55493867 @default.
- W1973680826 hasConcept C62520636 @default.
- W1973680826 hasConcept C62614982 @default.
- W1973680826 hasConcept C71240020 @default.
- W1973680826 hasConceptScore W1973680826C121332964 @default.
- W1973680826 hasConceptScore W1973680826C13965031 @default.
- W1973680826 hasConceptScore W1973680826C148898269 @default.
- W1973680826 hasConceptScore W1973680826C185592680 @default.
- W1973680826 hasConceptScore W1973680826C204328495 @default.
- W1973680826 hasConceptScore W1973680826C2776923230 @default.
- W1973680826 hasConceptScore W1973680826C55493867 @default.
- W1973680826 hasConceptScore W1973680826C62520636 @default.
- W1973680826 hasConceptScore W1973680826C62614982 @default.
- W1973680826 hasConceptScore W1973680826C71240020 @default.
- W1973680826 hasIssue "2" @default.
- W1973680826 hasLocation W19736808261 @default.
- W1973680826 hasLocation W19736808262 @default.
- W1973680826 hasOpenAccess W1973680826 @default.
- W1973680826 hasPrimaryLocation W19736808261 @default.
- W1973680826 hasRelatedWork W1591847193 @default.
- W1973680826 hasRelatedWork W1601666612 @default.
- W1973680826 hasRelatedWork W2012170330 @default.
- W1973680826 hasRelatedWork W2029939182 @default.
- W1973680826 hasRelatedWork W2057183688 @default.
- W1973680826 hasRelatedWork W2078317530 @default.
- W1973680826 hasRelatedWork W2079744596 @default.
- W1973680826 hasRelatedWork W2083019646 @default.
- W1973680826 hasRelatedWork W2206609427 @default.
- W1973680826 hasRelatedWork W3197201247 @default.
- W1973680826 hasVolume "391" @default.
- W1973680826 isParatext "false" @default.
- W1973680826 isRetracted "false" @default.
- W1973680826 magId "1973680826" @default.
- W1973680826 workType "article" @default.