FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2022763935> ?p ?o ?g. }

• W2022763935 endingPage "3161" @default.
• W2022763935 startingPage "3154" @default.
• W2022763935 abstract "When introduced into water, some molecules and ions (solutes) enforce the hydrogen-bonded network of neighboring water molecules that are thus restrained from thermal motions and are less mobile than those in the bulk phase (structure-making or positive hydration effect), and other solutes cause the opposite effect (structure-breaking or negative hydration effect). Using a method of microwave dielectric spectroscopy recently developed to measure the rotational mobility (dielectric relaxation frequency) of water hydrating proteins and the volume of hydration shells, the hydration of actin filament (F-actin) has been studied. The results indicate that F-actin exhibits both the structure-making and structure-breaking effects. Thus, apart from the water molecules with lowered rotational mobility that make up a typical hydration shell, there are other water molecules around the F-actin which have a much higher mobility than that of bulk water. No such dual hydration has been observed for myoglobin studied as the representative example of globular proteins which all showed qualitatively similar dielectric spectra. The volume fraction of the mobilized (hyper-mobile) water is roughly equal to that of the restrained water, which is two-thirds of the molecular volume of G-actin in size. The dielectric spectra of aqueous solutions of urea and potassium-halide salts have also been studied. The results suggest that urea and I− induce the hyper-mobile states of water, which is consistent with their well-known structure-breaking effect. The molecular surface of actin is rich in negative charges, which along with its filamentous structure provides a structural basis for the induction of a hyper-mobile state of water. A possible implication of the findings of the present study is discussed in relation to the chemomechanical energy transduction through interaction with myosin in the presence of ATP." @default.
• W2022763935 created "2016-06-24" @default.
• W2022763935 creator A5003464016 @default.
• W2022763935 creator A5021014908 @default.
• W2022763935 creator A5026230089 @default.
• W2022763935 creator A5064154990 @default.
• W2022763935 creator A5081577782 @default.
• W2022763935 date "2003-11-01" @default.
• W2022763935 modified "2023-10-12" @default.
• W2022763935 title "Hyper-Mobile Water Is Induced around Actin Filaments" @default.
• W2022763935 cites W1488840584 @default.
• W2022763935 cites W1538692246 @default.
• W2022763935 cites W1605294025 @default.
• W2022763935 cites W1972011607 @default.
• W2022763935 cites W1975727760 @default.
• W2022763935 cites W1976364866 @default.
• W2022763935 cites W197678773 @default.
• W2022763935 cites W1978601199 @default.
• W2022763935 cites W1981417623 @default.
• W2022763935 cites W1984717940 @default.
• W2022763935 cites W2010590930 @default.
• W2022763935 cites W2037940171 @default.
• W2022763935 cites W2040319470 @default.
• W2022763935 cites W2049098650 @default.
• W2022763935 cites W2053545079 @default.
• W2022763935 cites W2054135984 @default.
• W2022763935 cites W2055063842 @default.
• W2022763935 cites W2059757156 @default.
• W2022763935 cites W2069821109 @default.
• W2022763935 cites W2071328354 @default.
• W2022763935 cites W2079734282 @default.
• W2022763935 cites W2084233338 @default.
• W2022763935 cites W2090594901 @default.
• W2022763935 cites W2096677335 @default.
• W2022763935 cites W2126835369 @default.
• W2022763935 cites W2135372309 @default.
• W2022763935 cites W2150794610 @default.
• W2022763935 cites W2173549783 @default.
• W2022763935 cites W2325937979 @default.
• W2022763935 cites W4297917728 @default.
• W2022763935 doi "https://doi.org/10.1016/s0006-3495(03)74733-x" @default.
• W2022763935 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1303591" @default.
• W2022763935 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14581215" @default.
• W2022763935 hasPublicationYear "2003" @default.
• W2022763935 type Work @default.
• W2022763935 sameAs 2022763935 @default.
• W2022763935 citedByCount "88" @default.
• W2022763935 countsByYear W20227639352012 @default.
• W2022763935 countsByYear W20227639352013 @default.
• W2022763935 countsByYear W20227639352014 @default.
• W2022763935 countsByYear W20227639352015 @default.
• W2022763935 countsByYear W20227639352016 @default.
• W2022763935 countsByYear W20227639352017 @default.
• W2022763935 countsByYear W20227639352018 @default.
• W2022763935 countsByYear W20227639352019 @default.
• W2022763935 countsByYear W20227639352021 @default.
• W2022763935 countsByYear W20227639352022 @default.
• W2022763935 countsByYear W20227639352023 @default.
• W2022763935 crossrefType "journal-article" @default.
• W2022763935 hasAuthorship W2022763935A5003464016 @default.
• W2022763935 hasAuthorship W2022763935A5021014908 @default.
• W2022763935 hasAuthorship W2022763935A5026230089 @default.
• W2022763935 hasAuthorship W2022763935A5064154990 @default.
• W2022763935 hasAuthorship W2022763935A5081577782 @default.
• W2022763935 hasBestOaLocation W20227639351 @default.
• W2022763935 hasConcept C113196181 @default.
• W2022763935 hasConcept C125705527 @default.
• W2022763935 hasConcept C133386390 @default.
• W2022763935 hasConcept C14228908 @default.
• W2022763935 hasConcept C147789679 @default.
• W2022763935 hasConcept C148093993 @default.
• W2022763935 hasConcept C149823470 @default.
• W2022763935 hasConcept C159467904 @default.
• W2022763935 hasConcept C178790620 @default.
• W2022763935 hasConcept C179104552 @default.
• W2022763935 hasConcept C184651966 @default.
• W2022763935 hasConcept C185592680 @default.
• W2022763935 hasConcept C192562407 @default.
• W2022763935 hasConcept C2778063876 @default.
• W2022763935 hasConcept C32909587 @default.
• W2022763935 hasConcept C38743072 @default.
• W2022763935 hasConcept C49040817 @default.
• W2022763935 hasConcept C55493867 @default.
• W2022763935 hasConceptScore W2022763935C113196181 @default.
• W2022763935 hasConceptScore W2022763935C125705527 @default.
• W2022763935 hasConceptScore W2022763935C133386390 @default.
• W2022763935 hasConceptScore W2022763935C14228908 @default.
• W2022763935 hasConceptScore W2022763935C147789679 @default.
• W2022763935 hasConceptScore W2022763935C148093993 @default.
• W2022763935 hasConceptScore W2022763935C149823470 @default.
• W2022763935 hasConceptScore W2022763935C159467904 @default.
• W2022763935 hasConceptScore W2022763935C178790620 @default.
• W2022763935 hasConceptScore W2022763935C179104552 @default.
• W2022763935 hasConceptScore W2022763935C184651966 @default.
• W2022763935 hasConceptScore W2022763935C185592680 @default.
• W2022763935 hasConceptScore W2022763935C192562407 @default.
• W2022763935 hasConceptScore W2022763935C2778063876 @default.
• W2022763935 hasConceptScore W2022763935C32909587 @default.

• next