FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2072313812> ?p ?o ?g. }

• W2072313812 endingPage "10947" @default.
• W2072313812 startingPage "10934" @default.
• W2072313812 abstract "Conformational properties of the folded and unfolded ensembles of human interleukin-1 receptor antagonist (IL-1ra) are strongly denaturant-dependent as evidenced by high-resolution two-dimensional nuclear magnetic resonance (NMR), limited proteolysis, and small-angle X-ray scattering (SAXS). The folded ensemble was characterized in detail in the presence of different urea concentrations by (1)H-(15)N HSQC NMR. The beta-trefoil fold characteristic of native IL-1ra was preserved until the unfolding transition region beginning at 4 M urea. At the same time, a subset of native resonances disappeared gradually starting at low denaturant concentrations, indicating noncooperative changes in the folded state. Additional evidence of structural perturbations came from the chemical shift analysis, nonuniform and bell-shaped peak intensity profiles, and limited proteolysis. In particular, the following nearby regions of the tertiary structure became progressively destabilized with increasing urea concentrations: the beta-hairpin interface of trefoils 1 and 2 and the H2a-H2 helical region. These regions underwent small-scale perturbations within the native baseline region in the absence of populated molten globule-like states. Similar regions were affected by elevated temperatures known to induce irreversible aggregation of IL-1ra. Further evidence of structural transitions invoking near-native conformations came from an optical spectroscopy analysis of its single-tryptophan variant W17A. The increase in the radius of gyration was associated with a single equilibrium unfolding transition in the case of two different denaturants, urea and guanidine hydrochloride (GuHCl). However, the compactness of urea- and GuHCl-unfolded molecules was comparable only at high denaturant concentrations and deviated under less denaturing conditions. Our results identified the role of conformational flexibility in IL-1ra aggregation and shed light on the nature of structural transitions within the folded ensembles of other beta-trefoil proteins, such as IL-1beta and hFGF-1." @default.
• W2072313812 created "2016-06-24" @default.
• W2072313812 creator A5007060207 @default.
• W2072313812 creator A5011149614 @default.
• W2072313812 creator A5016754005 @default.
• W2072313812 creator A5033105906 @default.
• W2072313812 creator A5036143449 @default.
• W2072313812 creator A5051780803 @default.
• W2072313812 creator A5061250127 @default.
• W2072313812 creator A5082661305 @default.
• W2072313812 date "2009-10-29" @default.
• W2072313812 modified "2023-09-26" @default.
• W2072313812 title "Denaturant-Dependent Conformational Changes in a β-Trefoil Protein: Global and Residue-Specific Aspects of an Equilibrium Denaturation Process" @default.
• W2072313812 cites W1515255916 @default.
• W2072313812 cites W1515994079 @default.
• W2072313812 cites W1542001620 @default.
• W2072313812 cites W1849896198 @default.
• W2072313812 cites W1967154239 @default.
• W2072313812 cites W1972272379 @default.
• W2072313812 cites W1974027664 @default.
• W2072313812 cites W1974877835 @default.
• W2072313812 cites W1975715980 @default.
• W2072313812 cites W1977714757 @default.
• W2072313812 cites W1980076938 @default.
• W2072313812 cites W1983670463 @default.
• W2072313812 cites W1987992424 @default.
• W2072313812 cites W1989459539 @default.
• W2072313812 cites W1991746427 @default.
• W2072313812 cites W1996222219 @default.
• W2072313812 cites W2001149856 @default.
• W2072313812 cites W2001926601 @default.
• W2072313812 cites W2013270869 @default.
• W2072313812 cites W2017505620 @default.
• W2072313812 cites W2021006927 @default.
• W2072313812 cites W2027896662 @default.
• W2072313812 cites W2031612875 @default.
• W2072313812 cites W2036898162 @default.
• W2072313812 cites W2044625904 @default.
• W2072313812 cites W2045950270 @default.
• W2072313812 cites W2046912614 @default.
• W2072313812 cites W2046950192 @default.
• W2072313812 cites W2055882340 @default.
• W2072313812 cites W2056756454 @default.
• W2072313812 cites W2064446384 @default.
• W2072313812 cites W2066041565 @default.
• W2072313812 cites W2067884674 @default.
• W2072313812 cites W2069581195 @default.
• W2072313812 cites W2070432415 @default.
• W2072313812 cites W2070919406 @default.
• W2072313812 cites W2072927989 @default.
• W2072313812 cites W2073818426 @default.
• W2072313812 cites W2077707635 @default.
• W2072313812 cites W2080844007 @default.
• W2072313812 cites W2085895819 @default.
• W2072313812 cites W2089749221 @default.
• W2072313812 cites W2090751328 @default.
• W2072313812 cites W2095036416 @default.
• W2072313812 cites W2101781338 @default.
• W2072313812 cites W2107962592 @default.
• W2072313812 cites W2114304598 @default.
• W2072313812 cites W2116076986 @default.
• W2072313812 cites W2118167048 @default.
• W2072313812 cites W2122805799 @default.
• W2072313812 cites W2149877736 @default.
• W2072313812 cites W2157574830 @default.
• W2072313812 cites W2164670853 @default.
• W2072313812 cites W2169821755 @default.
• W2072313812 doi "https://doi.org/10.1021/bi901570k" @default.
• W2072313812 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19839644" @default.
• W2072313812 hasPublicationYear "2009" @default.
• W2072313812 type Work @default.
• W2072313812 sameAs 2072313812 @default.
• W2072313812 citedByCount "5" @default.
• W2072313812 countsByYear W20723138122012 @default.
• W2072313812 countsByYear W20723138122013 @default.
• W2072313812 countsByYear W20723138122014 @default.
• W2072313812 countsByYear W20723138122015 @default.
• W2072313812 countsByYear W20723138122022 @default.
• W2072313812 crossrefType "journal-article" @default.
• W2072313812 hasAuthorship W2072313812A5007060207 @default.
• W2072313812 hasAuthorship W2072313812A5011149614 @default.
• W2072313812 hasAuthorship W2072313812A5016754005 @default.
• W2072313812 hasAuthorship W2072313812A5033105906 @default.
• W2072313812 hasAuthorship W2072313812A5036143449 @default.
• W2072313812 hasAuthorship W2072313812A5051780803 @default.
• W2072313812 hasAuthorship W2072313812A5061250127 @default.
• W2072313812 hasAuthorship W2072313812A5082661305 @default.
• W2072313812 hasConcept C120665830 @default.
• W2072313812 hasConcept C121332964 @default.
• W2072313812 hasConcept C12554922 @default.
• W2072313812 hasConcept C131888329 @default.
• W2072313812 hasConcept C133571119 @default.
• W2072313812 hasConcept C13965031 @default.
• W2072313812 hasConcept C168568712 @default.
• W2072313812 hasConcept C175188612 @default.
• W2072313812 hasConcept C178790620 @default.
• W2072313812 hasConcept C185592680 @default.
• W2072313812 hasConcept C191486275 @default.

• next