title: Peptides in membranes: helicity and hydrophobicity.
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 alpha-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.
authors.affiliation: Division of Biochemistry Research, Hospital for Sick Children, Toronto, Ontario, Canada.
authors.forename: C M
authors.initials: CM
authors.lastname: Deber
authors.forename: S C
authors.initials: SC
authors.lastname: Li
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D002942:Circular Dichroism; D003196:Computer Graphics; D006860:Hydrogen Bonding; D008563:Membrane Lipids / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008567:Membranes, Artificial; D008823:Micelles; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D017433:Protein Structure, Secondary; D013696:Temperature; D013816:Thermodynamics
chemical_list: D000596:Amino Acids; D008563:Membrane Lipids; D008565:Membrane Proteins; D008567:Membranes, Artificial; D008823:Micelles; D010455:Peptides