Matches in SemOpenAlex for { <https://semopenalex.org/work/W1999989565> ?p ?o ?g. }
Showing items 1 to 81 of
81
with 100 items per page.
- W1999989565 endingPage "112a" @default.
- W1999989565 startingPage "112a" @default.
- W1999989565 abstract "In striated muscles contraction is regulated by the F-actin filament associated troponin-tropomyosin complex. Ca2+-binding to the N-terminal domain of troponin C (TnC) causes opening of that domain and exposure of the binding site for troponin I. To estimate the rate of this transition we have used a mutant of sTnC (TnC48/82) having Cys residues substituted for Gln48 in the B/C linker and Gln82 in helix D. These Cys residues are 4.4 Å and 14.3 Å apart (Cβ distance) in the closed and open domain conformation, respectively. Thus, they can readily form an intramolecular disulfide bond in the apo, but not in the Ca2+-bound state. We have evaluated the rates and the products of sTnC48/82 reaction with 5,5’-dithio-2-nitrobenzoic acid (DTNB) in a broad concentration range (0.05 - 50.0 mM). The reaction proceeds in two steps. First the thionitrobenzoic moiety is attached to one of the SH groups in a bimolecular disulfide exchange reaction. The second step is either an intramolecular disulfide exchange leading to crosslinking or blocking the remaining SH group with another bimolecular collision with DTNB. The ratio of the products is determined by urea-PAGE. We have found that in the absence of Ca2+ the reaction is slow and leads to 100% disulfide crosslinked product even at the highest DTNB concentrations. Addition of 1 mM CaCl2 causes a large (∼150 fold) increase in the rate of reaction, and surprisingly, at lower DTNB concentrations the protein is still efficiently crosslinked, despite its open conformation. Only at [DTNB]> 20 mM does rate of blocking the remaining Cys residue exceed that of intramolecular crosslinking. These results suggest that the regulatory domain of sTnC is very dynamic, a property that contributes to the rapid on-off switching of muscle contractile activity." @default.
- W1999989565 created "2016-06-24" @default.
- W1999989565 creator A5009756127 @default.
- W1999989565 creator A5019050254 @default.
- W1999989565 creator A5057429714 @default.
- W1999989565 date "2011-02-01" @default.
- W1999989565 modified "2023-09-26" @default.
- W1999989565 title "Conformational Dynamics of the Regulatory Domain of Troponin C" @default.
- W1999989565 doi "https://doi.org/10.1016/j.bpj.2010.12.820" @default.
- W1999989565 hasPublicationYear "2011" @default.
- W1999989565 type Work @default.
- W1999989565 sameAs 1999989565 @default.
- W1999989565 citedByCount "0" @default.
- W1999989565 crossrefType "journal-article" @default.
- W1999989565 hasAuthorship W1999989565A5009756127 @default.
- W1999989565 hasAuthorship W1999989565A5019050254 @default.
- W1999989565 hasAuthorship W1999989565A5057429714 @default.
- W1999989565 hasBestOaLocation W19999895651 @default.
- W1999989565 hasConcept C111919701 @default.
- W1999989565 hasConcept C115725540 @default.
- W1999989565 hasConcept C118552586 @default.
- W1999989565 hasConcept C12554922 @default.
- W1999989565 hasConcept C125705527 @default.
- W1999989565 hasConcept C133927893 @default.
- W1999989565 hasConcept C15744967 @default.
- W1999989565 hasConcept C181199279 @default.
- W1999989565 hasConcept C185592680 @default.
- W1999989565 hasConcept C205875245 @default.
- W1999989565 hasConcept C2776568683 @default.
- W1999989565 hasConcept C2777426643 @default.
- W1999989565 hasConcept C2780557392 @default.
- W1999989565 hasConcept C41008148 @default.
- W1999989565 hasConcept C500558357 @default.
- W1999989565 hasConcept C538909803 @default.
- W1999989565 hasConcept C55493867 @default.
- W1999989565 hasConcept C71240020 @default.
- W1999989565 hasConcept C75079739 @default.
- W1999989565 hasConcept C8010536 @default.
- W1999989565 hasConcept C86803240 @default.
- W1999989565 hasConceptScore W1999989565C111919701 @default.
- W1999989565 hasConceptScore W1999989565C115725540 @default.
- W1999989565 hasConceptScore W1999989565C118552586 @default.
- W1999989565 hasConceptScore W1999989565C12554922 @default.
- W1999989565 hasConceptScore W1999989565C125705527 @default.
- W1999989565 hasConceptScore W1999989565C133927893 @default.
- W1999989565 hasConceptScore W1999989565C15744967 @default.
- W1999989565 hasConceptScore W1999989565C181199279 @default.
- W1999989565 hasConceptScore W1999989565C185592680 @default.
- W1999989565 hasConceptScore W1999989565C205875245 @default.
- W1999989565 hasConceptScore W1999989565C2776568683 @default.
- W1999989565 hasConceptScore W1999989565C2777426643 @default.
- W1999989565 hasConceptScore W1999989565C2780557392 @default.
- W1999989565 hasConceptScore W1999989565C41008148 @default.
- W1999989565 hasConceptScore W1999989565C500558357 @default.
- W1999989565 hasConceptScore W1999989565C538909803 @default.
- W1999989565 hasConceptScore W1999989565C55493867 @default.
- W1999989565 hasConceptScore W1999989565C71240020 @default.
- W1999989565 hasConceptScore W1999989565C75079739 @default.
- W1999989565 hasConceptScore W1999989565C8010536 @default.
- W1999989565 hasConceptScore W1999989565C86803240 @default.
- W1999989565 hasIssue "3" @default.
- W1999989565 hasLocation W19999895651 @default.
- W1999989565 hasOpenAccess W1999989565 @default.
- W1999989565 hasPrimaryLocation W19999895651 @default.
- W1999989565 hasRelatedWork W162570409 @default.
- W1999989565 hasRelatedWork W1977082083 @default.
- W1999989565 hasRelatedWork W1977501908 @default.
- W1999989565 hasRelatedWork W1997149104 @default.
- W1999989565 hasRelatedWork W2008702688 @default.
- W1999989565 hasRelatedWork W2041405839 @default.
- W1999989565 hasRelatedWork W2045337689 @default.
- W1999989565 hasRelatedWork W2111903721 @default.
- W1999989565 hasRelatedWork W2418404888 @default.
- W1999989565 hasRelatedWork W4280546255 @default.
- W1999989565 hasVolume "100" @default.
- W1999989565 isParatext "false" @default.
- W1999989565 isRetracted "false" @default.
- W1999989565 magId "1999989565" @default.
- W1999989565 workType "article" @default.