FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2890819059> ?p ?o ?g. }

• W2890819059 endingPage "11430" @default.
• W2890819059 startingPage "11414" @default.
• W2890819059 abstract "Many unrelated proteins and peptides have been found spontaneously to form amyloid fibers above a critical concentration. Even for a single sequence, however, the amyloid fold is not a single well-defined structure. Although the cross-β hydrogen bonding pattern is common to all amyloids, all other aspects of amyloid fiber structures are sensitive to both the sequence of the aggregating peptides and the solvent conditions under which the aggregation occurs. Amyloid fibers are easy to identify and grossly characterize using microscopy, but their insolubility and aperiodicity along the dimensions transverse to the fiber axis have complicated detailed experimental structural characterization. In this paper, we explore the landscape of possibilities for amyloid protofilament structures that are made up of a single stack of peptides associated in a parallel in-register manner. We view this landscape as a two-dimensional version of the usual three-dimensional protein folding problem: the survey of the two-dimensional folds of protein ribbons. Adopting this view leads to a practical method of predicting stable protofilament structures of arbitrary sequences. We apply this scheme to variants of Aβ, the amyloid forming peptide that is characteristically associated with Alzheimer's disease. Consistent with what is known from experiment, we find that Aβ protofibrils are polymorphic. To our surprise, however, the ribbon-folding landscape of Aβ turned out to be strikingly simple. We confirm that, at the level of the monomeric protofilament, the landscape for the Aβ sequence is reasonably well funneled toward structures that are similar to those that have been determined by experiment. The landscape has more distinct minima than does a typical globular protein landscape but fewer and deeper minima than the landscape of a randomly shuffled sequence having the same overall composition. It is tempting to consider the possibility that the significant degree of funneling of Aβ's ribbon-folding landscape has arisen as a result of natural selection. More likely, however, the intermediate complexity of Aβ's ribbon-folding landscape has come from the post facto selection of the Aβ sequence as an object of study by researchers because only by having a landscape with some degree of funneling can ordered aggregation of such a peptide occur at in vivo concentrations. In addition to predicting polymorph structures, we show that predicted solubilities of polymorphs correlate with experiment and with their elongation free energies computed by coarse-grained molecular dynamics." @default.
• W2890819059 created "2018-09-27" @default.
• W2890819059 creator A5083686577 @default.
• W2890819059 creator A5088821383 @default.
• W2890819059 creator A5091808717 @default.
• W2890819059 date "2018-09-14" @default.
• W2890819059 modified "2023-09-24" @default.
• W2890819059 title "Surveying the Energy Landscapes of Aβ Fibril Polymorphism" @default.
• W2890819059 cites W1528511554 @default.
• W2890819059 cites W1961186421 @default.
• W2890819059 cites W1968253685 @default.
• W2890819059 cites W1972464683 @default.
• W2890819059 cites W1973978436 @default.
• W2890819059 cites W1982412808 @default.
• W2890819059 cites W1992898397 @default.
• W2890819059 cites W2001438084 @default.
• W2890819059 cites W2004098528 @default.
• W2890819059 cites W2011011528 @default.
• W2890819059 cites W2017684135 @default.
• W2890819059 cites W2019000267 @default.
• W2890819059 cites W2019465613 @default.
• W2890819059 cites W2024323623 @default.
• W2890819059 cites W2027058864 @default.
• W2890819059 cites W2027398076 @default.
• W2890819059 cites W2027839322 @default.
• W2890819059 cites W2033853317 @default.
• W2890819059 cites W2041250499 @default.
• W2890819059 cites W2043876754 @default.
• W2890819059 cites W2045820581 @default.
• W2890819059 cites W2052948216 @default.
• W2890819059 cites W2063679630 @default.
• W2890819059 cites W2066185874 @default.
• W2890819059 cites W2067214887 @default.
• W2890819059 cites W2080225612 @default.
• W2890819059 cites W2087357689 @default.
• W2890819059 cites W2087786915 @default.
• W2890819059 cites W2088079659 @default.
• W2890819059 cites W2091196473 @default.
• W2890819059 cites W2091938868 @default.
• W2890819059 cites W2094795801 @default.
• W2890819059 cites W2095215796 @default.
• W2890819059 cites W2095358223 @default.
• W2890819059 cites W2112154906 @default.
• W2890819059 cites W2121963977 @default.
• W2890819059 cites W2122191853 @default.
• W2890819059 cites W2140992384 @default.
• W2890819059 cites W2152580129 @default.
• W2890819059 cites W2153252106 @default.
• W2890819059 cites W2162741488 @default.
• W2890819059 cites W2163981524 @default.
• W2890819059 cites W2167954729 @default.
• W2890819059 cites W2171755502 @default.
• W2890819059 cites W2293372195 @default.
• W2890819059 cites W2319238142 @default.
• W2890819059 cites W2321913276 @default.
• W2890819059 cites W2327124850 @default.
• W2890819059 cites W2329336071 @default.
• W2890819059 cites W2407359553 @default.
• W2890819059 cites W2474799636 @default.
• W2890819059 cites W2495467174 @default.
• W2890819059 cites W2518672626 @default.
• W2890819059 cites W2529838384 @default.
• W2890819059 cites W2541594061 @default.
• W2890819059 cites W2542420667 @default.
• W2890819059 cites W2560598375 @default.
• W2890819059 cites W2571390534 @default.
• W2890819059 cites W2572424493 @default.
• W2890819059 cites W2600215207 @default.
• W2890819059 cites W2606208218 @default.
• W2890819059 cites W2753860285 @default.
• W2890819059 cites W2765872679 @default.
• W2890819059 cites W2766991252 @default.
• W2890819059 cites W2771052591 @default.
• W2890819059 cites W2774430028 @default.
• W2890819059 cites W2780468983 @default.
• W2890819059 cites W2787580408 @default.
• W2890819059 cites W2800227817 @default.
• W2890819059 cites W2806876262 @default.
• W2890819059 cites W2964220394 @default.
• W2890819059 doi "https://doi.org/10.1021/acs.jpcb.8b07364" @default.
• W2890819059 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6713213" @default.
• W2890819059 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30215519" @default.
• W2890819059 hasPublicationYear "2018" @default.
• W2890819059 type Work @default.
• W2890819059 sameAs 2890819059 @default.
• W2890819059 citedByCount "15" @default.
• W2890819059 countsByYear W28908190592019 @default.
• W2890819059 countsByYear W28908190592020 @default.
• W2890819059 countsByYear W28908190592021 @default.
• W2890819059 countsByYear W28908190592022 @default.
• W2890819059 countsByYear W28908190592023 @default.
• W2890819059 crossrefType "journal-article" @default.
• W2890819059 hasAuthorship W2890819059A5083686577 @default.
• W2890819059 hasAuthorship W2890819059A5088821383 @default.
• W2890819059 hasAuthorship W2890819059A5091808717 @default.
• W2890819059 hasBestOaLocation W28908190592 @default.
• W2890819059 hasConcept C119599485 @default.
• W2890819059 hasConcept C119621388 @default.

• next