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- W2003139512 abstract "Synthetic model membrane-interactive peptides—both of natural and designed sequence—have become convenient and systematic tools for determination of how the membrane-spanning segments within integral membrane proteins confer protein structure and biology. Conformational studies on these peptides demonstrate that the α-helix is the natural choice of conformation for a peptide segment in a membrane, and that a helical conformation will arise “automatically” in a peptide above a threshold hydrophobicity that allows it to associate stably with the membrane. Environmental and sequential contexts thus impart conformational versatility to many of the amino acids, thereby providing a mechanism for producing the diverse structural and functional properties of proteins. © 1994 John Wiley & Sons, Inc." @default.
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- W2003139512 date "1995-01-01" @default.
- W2003139512 modified "2023-10-17" @default.
- W2003139512 title "Peptides in membranes: Helicity and hydrophobicity" @default.
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