Peptides in membranes: helicity and hydrophobicity

Biopolymers. 1995;37(5):295-318. doi: 10.1002/bip.360370503.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / chemistry
  • Circular Dichroism
  • Computer Graphics
  • Hydrogen Bonding
  • Membrane Lipids / chemistry
  • Membrane Proteins / chemistry*
  • Membranes, Artificial*
  • Micelles
  • Models, Molecular
  • Molecular Sequence Data
  • Peptides / chemistry
  • Protein Structure, Secondary*
  • Temperature
  • Thermodynamics

Substances

  • Amino Acids
  • Membrane Lipids
  • Membrane Proteins
  • Membranes, Artificial
  • Micelles
  • Peptides