How hydrophobic interaction increases beta sheet protein?
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Hydrophobic interactions play a crucial role in increasing the stability of beta-sheet proteins. Research indicates that the folding of beta-sheets is primarily triggered by multistage hydrophobic interactions among neighboring side-chains of unfolded polypeptides, following explicit physical folding codes in aqueous environments . Molecular dynamics simulations show that extended conformations of peptides with large hydrophobic side chains can adopt beta-sheet conformations, with side chains interpenetrating each other, indicating the importance of hydrophobic forces in beta-sheet formation . Studies on amyloid peptides suggest that aromatic interactions are not strictly required for beta-sheet formation, as nonaromatic but highly hydrophobic residues can also lead to beta-sheet structures, highlighting the significant role of hydrophobicity in driving beta-sheet protein stability .
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| Papers (5) | Insight |
|---|---|
| Hydrophobic interaction with hydrophobic molecules like curcumin can increase the β-sheet proportion in yeast protein, as observed in the study on yeast protein interaction mechanisms. | |
100 Citations | Increasing hydrophobicity enhances beta-sheet protein self-assembly by promoting unique structural features and hydrogelation properties, as observed in the study on amphipathic peptides with varying hydrophobic residues. |
| Hydrophobic interactions promote beta-sheet formation by driving enthalpy in short sidechain sequences and entropy in large hydrophobic sidechain sequences, as observed in homodimeric peptide simulations. | |
40 Citations | Hydrophobic interactions in β-sheet formation are driven by enthalpy for short sidechains and entropy for large hydrophobic residues, influencing stability based on amino acid composition. |
Open access•Posted Content | Hydrophobic interactions among side-chains of adjacent beta-strands in beta-sheets trigger reproducible folding, following specific physical codes, due to a large hydrophobic surface area, aiding in protein folding. |
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