FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2073614644> ?p ?o ?g. }

• W2073614644 endingPage "1395" @default.
• W2073614644 startingPage "1386" @default.
• W2073614644 abstract "alpha-Tropomyosin (Tm) is a two-stranded alpha-helical coiled-coil protein, which participates in the regulation of muscle contraction. Unlike Tm purified from vertebrate muscle, recombinant Tm expressed in Escherichia coli is not acetylated at the N-terminal residue and loses the capacity to undergo head-to-tail polymerization, to bind actin and to inhibit actomyosin ATPase activity. These functions are restored by fusion of an N-terminal Ala-Ser (AS) dipeptide tail to recombinant Tm. Here, we have employed chemical (guanidine hydrochloride and urea) and physical (elevated hydrostatic pressures and low temperatures) denaturing agents to compare the structural stabilities of polymeric alanine-serine-tropomyosin (ASTm, containing the AS dipeptide) and dimeric non-fusion Tm (nfTm, i.e., not containing the AS dipeptide). Binding of the hydrophobic fluorescent dye bis-ANS, circular dichroism and size-exclusion chromatography were used to monitor the stabilities and state of association of both proteins under different solution conditions. Bis-ANS binding was markedly decreased at low concentrations (<1M) of GdnHCl or urea, whereas the secondary structures of both ASTm and nfTm were essentially unaffected in the same range of denaturant concentrations. These results suggest local unfolding of bis-ANS binding domains prior to global unfolding of Tm. In contrast, increased bis-ANS binding was observed when Tm was submitted to high pressures or to low temperatures, implying increased exposure of hydrophobic domains in the protein. Taken together, the different sensitivities of ASTm and nfTm to different denaturing agents support the notion that, at close to physiological conditions, head-to-tail interactions in polymerized ASTm are predominantly stabilized by electrostatic interactions between adjacent Tm dimers, whereas non-polar interactions appear to play a major role in the stability of the coiled-coil structure of individual Tm dimers." @default.
• W2073614644 created "2016-06-24" @default.
• W2073614644 creator A5044284195 @default.
• W2073614644 creator A5070851422 @default.
• W2073614644 date "2005-07-01" @default.
• W2073614644 modified "2023-09-25" @default.
• W2073614644 title "Folding and stability of a coiled-coil investigated using chemical and physical denaturing agents: Comparative analysis of polymerized and non-polymerized forms of α-tropomyosin" @default.
• W2073614644 cites W1481760785 @default.
• W2073614644 cites W1483681573 @default.
• W2073614644 cites W1484681199 @default.
• W2073614644 cites W1495869497 @default.
• W2073614644 cites W1505151868 @default.
• W2073614644 cites W1507475376 @default.
• W2073614644 cites W1518124859 @default.
• W2073614644 cites W1521831608 @default.
• W2073614644 cites W1747748421 @default.
• W2073614644 cites W1967802967 @default.
• W2073614644 cites W1970924050 @default.
• W2073614644 cites W1973887565 @default.
• W2073614644 cites W1977307506 @default.
• W2073614644 cites W1980581336 @default.
• W2073614644 cites W1991068914 @default.
• W2073614644 cites W2000802662 @default.
• W2073614644 cites W2000889585 @default.
• W2073614644 cites W2010891200 @default.
• W2073614644 cites W2014281089 @default.
• W2073614644 cites W2017331175 @default.
• W2073614644 cites W2017655053 @default.
• W2073614644 cites W2028569629 @default.
• W2073614644 cites W2029353291 @default.
• W2073614644 cites W2031321416 @default.
• W2073614644 cites W2038253226 @default.
• W2073614644 cites W2039839088 @default.
• W2073614644 cites W2043067395 @default.
• W2073614644 cites W2055883955 @default.
• W2073614644 cites W2061365077 @default.
• W2073614644 cites W2064674376 @default.
• W2073614644 cites W2064968634 @default.
• W2073614644 cites W2065547357 @default.
• W2073614644 cites W2067514010 @default.
• W2073614644 cites W2075642393 @default.
• W2073614644 cites W2082738681 @default.
• W2073614644 cites W2083998431 @default.
• W2073614644 cites W2089155927 @default.
• W2073614644 cites W2091186477 @default.
• W2073614644 cites W2105113617 @default.
• W2073614644 cites W2112336169 @default.
• W2073614644 cites W2113342629 @default.
• W2073614644 cites W2116441099 @default.
• W2073614644 cites W2127625548 @default.
• W2073614644 cites W2162875257 @default.
• W2073614644 cites W2332193780 @default.
• W2073614644 cites W2435566390 @default.
• W2073614644 cites W4299496276 @default.
• W2073614644 cites W952792670 @default.
• W2073614644 doi "https://doi.org/10.1016/j.biocel.2005.01.008" @default.
• W2073614644 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15833271" @default.
• W2073614644 hasPublicationYear "2005" @default.
• W2073614644 type Work @default.
• W2073614644 sameAs 2073614644 @default.
• W2073614644 citedByCount "7" @default.
• W2073614644 countsByYear W20736146442016 @default.
• W2073614644 crossrefType "journal-article" @default.
• W2073614644 hasAuthorship W2073614644A5044284195 @default.
• W2073614644 hasAuthorship W2073614644A5070851422 @default.
• W2073614644 hasConcept C12554922 @default.
• W2073614644 hasConcept C125705527 @default.
• W2073614644 hasConcept C133571119 @default.
• W2073614644 hasConcept C13965031 @default.
• W2073614644 hasConcept C178790620 @default.
• W2073614644 hasConcept C181199279 @default.
• W2073614644 hasConcept C185592680 @default.
• W2073614644 hasConcept C193363816 @default.
• W2073614644 hasConcept C19472624 @default.
• W2073614644 hasConcept C205875245 @default.
• W2073614644 hasConcept C2776923230 @default.
• W2073614644 hasConcept C2779138802 @default.
• W2073614644 hasConcept C2779281246 @default.
• W2073614644 hasConcept C2779463914 @default.
• W2073614644 hasConcept C44228677 @default.
• W2073614644 hasConcept C521977710 @default.
• W2073614644 hasConcept C55493867 @default.
• W2073614644 hasConcept C55988834 @default.
• W2073614644 hasConcept C62614982 @default.
• W2073614644 hasConcept C75599170 @default.
• W2073614644 hasConcept C8010536 @default.
• W2073614644 hasConcept C86803240 @default.
• W2073614644 hasConceptScore W2073614644C12554922 @default.
• W2073614644 hasConceptScore W2073614644C125705527 @default.
• W2073614644 hasConceptScore W2073614644C133571119 @default.
• W2073614644 hasConceptScore W2073614644C13965031 @default.
• W2073614644 hasConceptScore W2073614644C178790620 @default.
• W2073614644 hasConceptScore W2073614644C181199279 @default.
• W2073614644 hasConceptScore W2073614644C185592680 @default.
• W2073614644 hasConceptScore W2073614644C193363816 @default.
• W2073614644 hasConceptScore W2073614644C19472624 @default.
• W2073614644 hasConceptScore W2073614644C205875245 @default.
• W2073614644 hasConceptScore W2073614644C2776923230 @default.

• next