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- W100593479 abstract "Two new amphipathy scales elaborated from molecular dynamics data are presented. Their applications contribute for the identification of the hydrophobic or hydrophilic regions in proteins solely from the primary structure. The new amphipathy coefficients (AC) reflect the side chain/solvent molecules configurational energies. A polar (water) and an apolar solvent, CCl4, were used resulting in the two ACwater and ACCCl4 scales. These solvents were chosen to simulate the aqueous phases and the transmembrane ambients of cellular membranes where the membrane proteins act. The new amphipathy scales were compared with some previous scales determined by different methods, which were also compared between them, indicating more than 90% of the correlation coefficients are less than 0.9: the scales are strictly dependent on the methodologies used in their determination. The ACCCl4 scale is related with the size of side chain amino acids while ACwater is related with the hydrophobicity of side chain amino acids. The quality of the scales was confirmed by an example of application where ACwater was able to identify correctly the transmembrane, hydrophobic regions of a membrane protein. These results also indicate that water is an important factor responsible for the tertiary structure of membrane proteins." @default.
- W100593479 created "2016-06-24" @default.
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- W100593479 date "2005-02-01" @default.
- W100593479 modified "2023-10-17" @default.
- W100593479 title "A new amphipathy scale" @default.
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- W100593479 doi "https://doi.org/10.1016/j.bbapap.2004.09.019" @default.
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