An amphipathic alpha-helix at a membrane interface: a structural study using a novel X-ray diffraction method.

  title={An amphipathic alpha-helix at a membrane interface: a structural study using a novel X-ray diffraction method.},
  author={Kalina Hristova and William C. Wimley and Vinod K. Mishra and G M Anantharamiah and Jere P. Segrest and Stephen H White},
  journal={Journal of molecular biology},
  volume={290 1},
The amphipathic alpha-helix is a recurrent feature of membrane-active proteins, peptides, and toxins. Despite extensive biophysical studies, the structural details of its affinity for membrane interfaces remain rather vague. We report here the first results of an effort to obtain detailed structural information about alpha-helices in membranes by means of a novel X-ray diffraction method. Specifically, we determined the transbilayer position and orientation of an archetypal class A amphipathic… 
Peptides in Lipid Bilayers: Determination of Location by Absolute-Scale X-ray Refinement
This chapter shows how absolute-scale refinement can be used to obtain quantitative information about the position, orientation, and conformation of a helical peptide in a fluid lipid bilayer and about the perturbations of the bilayer structure caused by the peptide.
Site-specific tryptophan dynamics in class A amphipathic helical peptides at a phospholipid bilayer interface.
A general amphipathic α-helical motif for sensing membrane curvature
An algorithm is built to identify other potential amphipathic α-helices rich in serine and threonine residues in protein databases, and shows that three act as membrane curvature sensors.
Association of a model class A (apolipoprotein) amphipathic alpha helical peptide with lipid: high resolution NMR studies of peptide.lipid discoidal complexes.
High resolution NMR studies deduce detailed structure of recombinant peptide and propose that peptide helices are arranged in a head to tail fashion to cover the edge of the disc, consistent with the pKa values of the Lys residues determined previously.
Structure, location, and lipid perturbations of melittin at the membrane interface.
An amphipathic alpha-helical peptide from apolipoprotein A1 stabilizes protein polymer vesicles.
Folding of beta-sheets in membranes: specificity and promiscuity in peptide model systems.
The results support the idea that the predominant interactions of the side-chains in membrane-bound beta-sheets are with the membrane lipids, and that backbone hydrogen bonding is the major driving force for the stabilization of beta-sheet formation in membranes.
Protein folding in membranes: insights from neutron diffraction studies of a membrane beta-sheet oligomer.
Studies of the assembly of the hexapeptide Acetyl-Trp-Leu(5) (AcWL(5)) into beta-sheets in membranes have provided insights into membrane protein folding. Yet, the exact structure of the oligomer in
Perturbation of a lipid membrane by amphipathic peptides and its role in pore formation
It is shown that the membrane perturbation free energy depends critically on peptide orientation: in the transmembrane pore state the lipid perturbations energy, per peptide, is smaller than in the adsorbed state, which suggests that the gain in conformational freedom of the lipid chains is a central driving force for pore formation.
Chapter III Interactions of Fusogenic Coiled-Coil Lipopeptides with Zwitterionic Lipid Monolayers: Implications for Lipopeptide Mediated Vesicle Fusion
  • Biology, Chemistry
  • 2015
Light is shed on important mechanistic details of the membrane fusion process in this model system that models the key features of this process and will help the rational design of new artificial membrane fusion systems, which have a wide range of potential applications in supramolecular chemistry and biomedicine.


The amphipathic helix in the exchangeable apolipoproteins: a review of secondary structure and function.
It is of particular interest, therefore, that all of the exchangeable apolipoproteins except apoA-II and C-I, contain amphipathic helixes of class G*.
The structure and orientation of class-A amphipathic peptides on a phospholipid bilayer surface
It is concluded that these class A amphipathic peptides lie parallel to the lipid surface and penetrate no deeper than the ester linkages of the phospholipids.
Microenvironments of basic amino acids in amphipathic alpha-helices bound to phospholipid: 13C NMR studies using selectively labeled peptides.
The lipid-binding properties of serum apolipoproteins are mediated by class A amphipathic alpha-helices in which basic and acidic amino acid residues tend to be localized at the helix polar-nonpolar
Conformational analysis of lipid-associating proteins in a lipid environment.
Studies of synthetic peptide analogs of the amphipathic helix. Structure of complexes with dimyristoyl phosphatidylcholine.
The Amphipathic Helix
The Amphipathic Helix as a Structural Feature Involved in T-Cell Recognition and other Biological Roles for AmphipATHic Helices in Membrane-Related Phenomenon are outlined.
Differentiation of lipid-associating helices by use of three-dimensional molecular hydrophobicity potential calculations.
  • R. Brasseur
  • Biology, Chemistry
    The Journal of biological chemistry
  • 1991
Computer programs to identify and classify amphipathic alpha helical domains.
Five computer programs that automate analysis and classification of potential amphipathic helical domains from primary amino acid sequence data are developed and used to localize and characterize the putative amphipATHic helixes in the exchangeable apolipoproteins.