Matches in SemOpenAlex for { <https://semopenalex.org/work/W1975026433> ?p ?o ?g. }
- W1975026433 endingPage "13050" @default.
- W1975026433 startingPage "13040" @default.
- W1975026433 abstract "A common strategy to study the mechanism of amyloid formation is the characterization of the structure and dynamics of the precursor state, which is in most cases a partially folded protein. Here we investigated the highly dynamic conformational state formed by the protein domain HypF-N at low pH, before aggregation, using fluorescence, circular dichroism, and NMR spectroscopies. The NMR analysis allowed us, in particular, to identify the regions of the sequence that form hydrophobic interactions and adopt an α-helical secondary structure in the pH-denatured ensemble. To understand the role that this residual structure plays in the aggregation of this protein, we probed the mechanism of aggregation using protein engineering experiments and thus identified the regions of the sequence of HypF-N that play a critical role in the conversion of this dynamic state into thioflavin T-binding and β-sheet containing protofibrils. The combination of these two complementary approaches revealed that the aggregation of pH-denatured HypF-N is not structure-dependent, meaning that it is not driven by the regions of the protein that are either less or more protected in the initial partially folded state. It is, by contrast, promoted by discrete protein regions that have the highest intrinsic propensity to aggregate because of their physicochemical properties." @default.
- W1975026433 created "2016-06-24" @default.
- W1975026433 creator A5004511581 @default.
- W1975026433 creator A5030911157 @default.
- W1975026433 creator A5030913259 @default.
- W1975026433 creator A5032721511 @default.
- W1975026433 creator A5038452125 @default.
- W1975026433 creator A5059438841 @default.
- W1975026433 creator A5060606224 @default.
- W1975026433 creator A5062473197 @default.
- W1975026433 creator A5075804077 @default.
- W1975026433 date "2008-09-04" @default.
- W1975026433 modified "2023-10-10" @default.
- W1975026433 title "Structure and Dynamics of a Partially Folded Protein Are Decoupled from Its Mechanism of Aggregation" @default.
- W1975026433 cites W1188919047 @default.
- W1975026433 cites W1680110353 @default.
- W1975026433 cites W1710827023 @default.
- W1975026433 cites W1969846705 @default.
- W1975026433 cites W1973680007 @default.
- W1975026433 cites W1976201852 @default.
- W1975026433 cites W1977846417 @default.
- W1975026433 cites W1980125299 @default.
- W1975026433 cites W1985297174 @default.
- W1975026433 cites W1988624456 @default.
- W1975026433 cites W1989780699 @default.
- W1975026433 cites W1994907993 @default.
- W1975026433 cites W1996518756 @default.
- W1975026433 cites W2000659036 @default.
- W1975026433 cites W2002195659 @default.
- W1975026433 cites W2009890105 @default.
- W1975026433 cites W2017129714 @default.
- W1975026433 cites W2021332309 @default.
- W1975026433 cites W2023913847 @default.
- W1975026433 cites W2025112049 @default.
- W1975026433 cites W2033798316 @default.
- W1975026433 cites W2033847972 @default.
- W1975026433 cites W2038694710 @default.
- W1975026433 cites W2038729585 @default.
- W1975026433 cites W2041445887 @default.
- W1975026433 cites W2044448989 @default.
- W1975026433 cites W2046014998 @default.
- W1975026433 cites W2049708286 @default.
- W1975026433 cites W2051651977 @default.
- W1975026433 cites W2052660967 @default.
- W1975026433 cites W2053164047 @default.
- W1975026433 cites W2060215277 @default.
- W1975026433 cites W2063067093 @default.
- W1975026433 cites W2065259975 @default.
- W1975026433 cites W2067214887 @default.
- W1975026433 cites W2071982060 @default.
- W1975026433 cites W2073623519 @default.
- W1975026433 cites W2075454119 @default.
- W1975026433 cites W2076834744 @default.
- W1975026433 cites W2080399081 @default.
- W1975026433 cites W2091311712 @default.
- W1975026433 cites W2092356013 @default.
- W1975026433 cites W2093861673 @default.
- W1975026433 cites W2094118845 @default.
- W1975026433 cites W2096192349 @default.
- W1975026433 cites W2107904341 @default.
- W1975026433 cites W2114078421 @default.
- W1975026433 cites W2115556862 @default.
- W1975026433 cites W2118280241 @default.
- W1975026433 cites W2120717592 @default.
- W1975026433 cites W2121963977 @default.
- W1975026433 cites W2122294662 @default.
- W1975026433 cites W2140389961 @default.
- W1975026433 cites W2157842863 @default.
- W1975026433 cites W2164233055 @default.
- W1975026433 cites W2165186407 @default.
- W1975026433 cites W2169707043 @default.
- W1975026433 cites W2169821755 @default.
- W1975026433 cites W4244624346 @default.
- W1975026433 doi "https://doi.org/10.1021/ja8029224" @default.
- W1975026433 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18767849" @default.
- W1975026433 hasPublicationYear "2008" @default.
- W1975026433 type Work @default.
- W1975026433 sameAs 1975026433 @default.
- W1975026433 citedByCount "36" @default.
- W1975026433 countsByYear W19750264332012 @default.
- W1975026433 countsByYear W19750264332013 @default.
- W1975026433 countsByYear W19750264332014 @default.
- W1975026433 countsByYear W19750264332015 @default.
- W1975026433 countsByYear W19750264332016 @default.
- W1975026433 countsByYear W19750264332018 @default.
- W1975026433 countsByYear W19750264332019 @default.
- W1975026433 countsByYear W19750264332021 @default.
- W1975026433 crossrefType "journal-article" @default.
- W1975026433 hasAuthorship W1975026433A5004511581 @default.
- W1975026433 hasAuthorship W1975026433A5030911157 @default.
- W1975026433 hasAuthorship W1975026433A5030913259 @default.
- W1975026433 hasAuthorship W1975026433A5032721511 @default.
- W1975026433 hasAuthorship W1975026433A5038452125 @default.
- W1975026433 hasAuthorship W1975026433A5059438841 @default.
- W1975026433 hasAuthorship W1975026433A5060606224 @default.
- W1975026433 hasAuthorship W1975026433A5062473197 @default.
- W1975026433 hasAuthorship W1975026433A5075804077 @default.
- W1975026433 hasConcept C12554922 @default.