Matches in SemOpenAlex for { <https://semopenalex.org/work/W2004356290> ?p ?o ?g. }
Showing items 1 to 81 of
81
with 100 items per page.
- W2004356290 endingPage "11576" @default.
- W2004356290 startingPage "11568" @default.
- W2004356290 abstract "In this work, we study the kinetics of the R → T transition in hemoglobin using a combination of near-infrared and near-ultraviolet spectroscopy. We use a sol−gel encapsulation protocol to decelerate the conformational transitions and to avoid spectral perturbations arising from ligand migration and recombination. We monitor two spectroscopic markers: band III in the near-IR, which is a fine probe of the heme pocket conformation, and the tryptophan band in the near-UV, which probes the formation of the Trpβ37−Aspα94 hydrogen bond, characteristic of the T structure, at the critical α1β2 subunit interface. The time evolution of these two bands is monitored after deoxygenation of encapsulated oxyhemoglobin, obtained by diffusion of a reducing agent into the porous silica matrix. Characteristic spectral shifts are observed: comparison with myoglobin enables us to assign them to quaternary structure relaxations. Band III spectral relaxation is clearly nonexponential, and analysis with the Maximum Entropy Method enables us to identify three processes. On the other hand, near-UV spectral relaxation follows an exponential decay with a time constant closely corresponding to the second process observed in the near IR. Very interestingly, the rates of all processes markedly depend on the viscosity of the co-encapsulated solvent, following a power law. Our results reveal correlations between heme pocket relaxations, induced by the R → T transition, and structural event(s) occurring at the α1β2 interface and highlight their solvent dependence. The power law viscosity dependence of relaxation rates suggests that the observed protein relaxations are “slaved” to the co-encapsulated solvent. The stepwise character of the quaternary transition is also evidenced." @default.
- W2004356290 created "2016-06-24" @default.
- W2004356290 creator A5023887372 @default.
- W2004356290 creator A5091296060 @default.
- W2004356290 date "2007-09-19" @default.
- W2004356290 modified "2023-10-13" @default.
- W2004356290 title "Quaternary Relaxations in Sol−Gel Encapsulated Hemoglobin Studied via NIR and UV Spectroscopy" @default.
- W2004356290 cites W1579947842 @default.
- W2004356290 cites W1948960263 @default.
- W2004356290 cites W1964900390 @default.
- W2004356290 cites W1966600252 @default.
- W2004356290 cites W1973110977 @default.
- W2004356290 cites W1974139041 @default.
- W2004356290 cites W2004194157 @default.
- W2004356290 cites W2007673127 @default.
- W2004356290 cites W2015894243 @default.
- W2004356290 cites W2020601552 @default.
- W2004356290 cites W2020904151 @default.
- W2004356290 cites W2029718053 @default.
- W2004356290 cites W2032372720 @default.
- W2004356290 cites W2059686384 @default.
- W2004356290 cites W2078502772 @default.
- W2004356290 cites W2087554741 @default.
- W2004356290 cites W2089727977 @default.
- W2004356290 cites W2120135466 @default.
- W2004356290 cites W2125087906 @default.
- W2004356290 cites W2146334532 @default.
- W2004356290 doi "https://doi.org/10.1021/bi701166m" @default.
- W2004356290 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17880111" @default.
- W2004356290 hasPublicationYear "2007" @default.
- W2004356290 type Work @default.
- W2004356290 sameAs 2004356290 @default.
- W2004356290 citedByCount "19" @default.
- W2004356290 countsByYear W20043562902012 @default.
- W2004356290 countsByYear W20043562902013 @default.
- W2004356290 countsByYear W20043562902015 @default.
- W2004356290 countsByYear W20043562902019 @default.
- W2004356290 countsByYear W20043562902022 @default.
- W2004356290 crossrefType "journal-article" @default.
- W2004356290 hasAuthorship W2004356290A5023887372 @default.
- W2004356290 hasAuthorship W2004356290A5091296060 @default.
- W2004356290 hasConcept C112887158 @default.
- W2004356290 hasConcept C121332964 @default.
- W2004356290 hasConcept C148898269 @default.
- W2004356290 hasConcept C178790620 @default.
- W2004356290 hasConcept C185592680 @default.
- W2004356290 hasConcept C2778063876 @default.
- W2004356290 hasConcept C32891209 @default.
- W2004356290 hasConcept C32909587 @default.
- W2004356290 hasConcept C62520636 @default.
- W2004356290 hasConceptScore W2004356290C112887158 @default.
- W2004356290 hasConceptScore W2004356290C121332964 @default.
- W2004356290 hasConceptScore W2004356290C148898269 @default.
- W2004356290 hasConceptScore W2004356290C178790620 @default.
- W2004356290 hasConceptScore W2004356290C185592680 @default.
- W2004356290 hasConceptScore W2004356290C2778063876 @default.
- W2004356290 hasConceptScore W2004356290C32891209 @default.
- W2004356290 hasConceptScore W2004356290C32909587 @default.
- W2004356290 hasConceptScore W2004356290C62520636 @default.
- W2004356290 hasIssue "41" @default.
- W2004356290 hasLocation W20043562901 @default.
- W2004356290 hasLocation W20043562902 @default.
- W2004356290 hasOpenAccess W2004356290 @default.
- W2004356290 hasPrimaryLocation W20043562901 @default.
- W2004356290 hasRelatedWork W1531601525 @default.
- W2004356290 hasRelatedWork W2319480705 @default.
- W2004356290 hasRelatedWork W2384464875 @default.
- W2004356290 hasRelatedWork W2606230654 @default.
- W2004356290 hasRelatedWork W2607424097 @default.
- W2004356290 hasRelatedWork W2748952813 @default.
- W2004356290 hasRelatedWork W2899084033 @default.
- W2004356290 hasRelatedWork W2948807893 @default.
- W2004356290 hasRelatedWork W4387497383 @default.
- W2004356290 hasRelatedWork W2778153218 @default.
- W2004356290 hasVolume "46" @default.
- W2004356290 isParatext "false" @default.
- W2004356290 isRetracted "false" @default.
- W2004356290 magId "2004356290" @default.
- W2004356290 workType "article" @default.