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- W2023342552 abstract "The chain-length dependence of the alpha-helix to beta-sheet transition in poly(L-lysine) is studied by temperature-tuned FTIR spectroscopy. This study shows that heterogeneous samples of poly(L-lysine), comprising polypeptide chains with various lengths, undergo the alpha-beta transition at an intermediate temperature compared to homogeneous ingredients. This holds true as long as each individual fraction of the polypeptide is capable of adopting an antiparallel beta-sheet structure. The tendency is that the longer chain is, the lower the alpha-beta transition temperature is, which has been linked to the presence of distorted or solvated helices with turns or beta sheets in elongating chains of poly(L-lysine). As such helical structures are apparently conducive to the alpha-beta transition, this draws a comparison to the hypothesis of metastable protein conformational states being a common stage in amyloid-formation pathways. The antiparallel architecture of the beta sheet is likely to reflect the pretransition interhelical interactions in poly(L-lysine). Namely, the chains are arranged in an antiparallel manner because of energetically favored antiparallel pre-assembly of dipolar alpha helices." @default.
- W2023342552 created "2016-06-24" @default.
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- W2023342552 creator A5056907141 @default.
- W2023342552 date "2004-01-28" @default.
- W2023342552 modified "2023-10-09" @default.
- W2023342552 title "Chain‐length dependence of α‐helix to β‐sheet transition in polylysine: Model of protein aggregation studied by temperature‐tuned FTIR spectroscopy" @default.
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- W2023342552 doi "https://doi.org/10.1002/bip.10582" @default.
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