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- W2897762555 abstract "Significance Macromolecular crowding influences protein−protein interactions via hard-core repulsions and chemical interactions. Scaled particle theory predicts that the effect of hard-core repulsions depends on the shape of the protein complex, and simple ideas about chemical interactions predict a dominant role for the chemical qualities of the protein surface. The theory predicts that a collapsed, ellipsoidal, dimer will be stabilized by hard-core repulsions, whereas a less collapsed, side-by-side, dimer will not. We applied scaled particle theory to two dimers with nearly identical surfaces but different shapes. Our results support the predictions; crowders that interact primarily through hard-core repulsions stabilize the ellipsoidal domain-swapped dimer more than the side-by-side dimer, whereas crowders that interact via chemical interactions have the same effect on both dimers." @default.
- W2897762555 created "2018-10-26" @default.
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- W2897762555 date "2018-10-09" @default.
- W2897762555 modified "2023-10-17" @default.
- W2897762555 title "Protein shape modulates crowding effects" @default.
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- W2897762555 doi "https://doi.org/10.1073/pnas.1810054115" @default.
- W2897762555 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6205421" @default.
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