Matches in SemOpenAlex for { <https://semopenalex.org/work/W1966474967> ?p ?o ?g. }
Showing items 1 to 81 of
81
with 100 items per page.
- W1966474967 endingPage "725" @default.
- W1966474967 startingPage "713" @default.
- W1966474967 abstract "Disulfide bonds in a folding protein chain are equivalent to prematurely formed native-like tertiary interactions. We investigated whether the mechanism of protein folding is changed by the presence of disulfide bonds. As a model we used the S54G/P55N-variant of ribonuclease T1, a protein with two disulfide bonds and a single cis proline (Pro39), and we measured both the direct and the proline-limited folding reactions before and after breaking of the disulfide bonds. The folding kinetics were compared under refolding conditions, in the regions of the area-induced unfolding transitions of the two forms, and under folding conditions. The kinetics in the transition regions were analyzed on the basis of a three-species mechanism and all microscopic rate constants of folding and of prolyl isomerization could be determined as a function of the area concentration from the measured rates and amplitudes. These kinetic analyses indicated that the disulfide bonds can be rather unfavorable for the folding of S54G/P55N-ribonuclease T1. Under strongly native conditions they retard the rate-limiting trans→cis isomerization of Pro39 because they allow the rapid formation of partially ordered structure prior to the proline-limited refolding reaction. Under unfolding conditions the isomerization of Pro39 is not affected. The direct unfolding and refolding reactions in the transition region of polypeptide chains with correct prolyl isomers are also decelerated when the disulfide bonds are present. These changes in the folding kinetics are possibly related to the decrease in chain flexibility that is caused by the disulfide bonds. A high flexibility is probably important throughout folding, and in the case of ribonuclease T1 a premature locking of tertiary contacts by intact disulfide bonds can interfere unfavorably with both the direct and the proline-limited folding reactions." @default.
- W1966474967 created "2016-06-24" @default.
- W1966474967 creator A5003613610 @default.
- W1966474967 creator A5004538725 @default.
- W1966474967 date "1994-06-01" @default.
- W1966474967 modified "2023-09-23" @default.
- W1966474967 title "Intact Disulfide Bonds Decelerate the Folding of Ribonuclease T1" @default.
- W1966474967 doi "https://doi.org/10.1006/jmbi.1994.1408" @default.
- W1966474967 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8014991" @default.
- W1966474967 hasPublicationYear "1994" @default.
- W1966474967 type Work @default.
- W1966474967 sameAs 1966474967 @default.
- W1966474967 citedByCount "56" @default.
- W1966474967 countsByYear W19664749672012 @default.
- W1966474967 countsByYear W19664749672013 @default.
- W1966474967 countsByYear W19664749672017 @default.
- W1966474967 crossrefType "journal-article" @default.
- W1966474967 hasAuthorship W1966474967A5003613610 @default.
- W1966474967 hasAuthorship W1966474967A5004538725 @default.
- W1966474967 hasConcept C104317684 @default.
- W1966474967 hasConcept C119599485 @default.
- W1966474967 hasConcept C121332964 @default.
- W1966474967 hasConcept C126661725 @default.
- W1966474967 hasConcept C127413603 @default.
- W1966474967 hasConcept C148898269 @default.
- W1966474967 hasConcept C161790260 @default.
- W1966474967 hasConcept C162203774 @default.
- W1966474967 hasConcept C178790620 @default.
- W1966474967 hasConcept C185592680 @default.
- W1966474967 hasConcept C204328495 @default.
- W1966474967 hasConcept C27256138 @default.
- W1966474967 hasConcept C2776545253 @default.
- W1966474967 hasConcept C2778976237 @default.
- W1966474967 hasConcept C5098756 @default.
- W1966474967 hasConcept C55493867 @default.
- W1966474967 hasConcept C62520636 @default.
- W1966474967 hasConcept C67705224 @default.
- W1966474967 hasConcept C71240020 @default.
- W1966474967 hasConcept C8010536 @default.
- W1966474967 hasConceptScore W1966474967C104317684 @default.
- W1966474967 hasConceptScore W1966474967C119599485 @default.
- W1966474967 hasConceptScore W1966474967C121332964 @default.
- W1966474967 hasConceptScore W1966474967C126661725 @default.
- W1966474967 hasConceptScore W1966474967C127413603 @default.
- W1966474967 hasConceptScore W1966474967C148898269 @default.
- W1966474967 hasConceptScore W1966474967C161790260 @default.
- W1966474967 hasConceptScore W1966474967C162203774 @default.
- W1966474967 hasConceptScore W1966474967C178790620 @default.
- W1966474967 hasConceptScore W1966474967C185592680 @default.
- W1966474967 hasConceptScore W1966474967C204328495 @default.
- W1966474967 hasConceptScore W1966474967C27256138 @default.
- W1966474967 hasConceptScore W1966474967C2776545253 @default.
- W1966474967 hasConceptScore W1966474967C2778976237 @default.
- W1966474967 hasConceptScore W1966474967C5098756 @default.
- W1966474967 hasConceptScore W1966474967C55493867 @default.
- W1966474967 hasConceptScore W1966474967C62520636 @default.
- W1966474967 hasConceptScore W1966474967C67705224 @default.
- W1966474967 hasConceptScore W1966474967C71240020 @default.
- W1966474967 hasConceptScore W1966474967C8010536 @default.
- W1966474967 hasIssue "5" @default.
- W1966474967 hasLocation W19664749671 @default.
- W1966474967 hasLocation W19664749672 @default.
- W1966474967 hasOpenAccess W1966474967 @default.
- W1966474967 hasPrimaryLocation W19664749671 @default.
- W1966474967 hasRelatedWork W1493551487 @default.
- W1966474967 hasRelatedWork W1994827273 @default.
- W1966474967 hasRelatedWork W2011823820 @default.
- W1966474967 hasRelatedWork W2014166768 @default.
- W1966474967 hasRelatedWork W2036898162 @default.
- W1966474967 hasRelatedWork W2052614246 @default.
- W1966474967 hasRelatedWork W2101262426 @default.
- W1966474967 hasRelatedWork W2131604629 @default.
- W1966474967 hasRelatedWork W2171985964 @default.
- W1966474967 hasRelatedWork W2749620357 @default.
- W1966474967 hasVolume "239" @default.
- W1966474967 isParatext "false" @default.
- W1966474967 isRetracted "false" @default.
- W1966474967 magId "1966474967" @default.
- W1966474967 workType "article" @default.