Christopher E. Dempsey

TL;DR: Despite the structural complexity of integral membrane proteins, it is interesting that in some respects their study be more straightforward, lacking as they do the elusive properties of melittin which limit the possibility of defining their interaction with membranes in terms of a single conformation, location, orientation and association state within the membrane.

TL;DR: Site-specific mutagenesis shows that a methionine residue, previously implicated as a potential interfacial residue, can be replaced with other hydrophobic residues without disrupting dimerization, suggesting a high degree of specificity in the helix-helix interactions.

TL;DR: The weak hydration of these Denaturant ions strongly supports suggestions that a major contribution to the denaturant effect is the preferential interaction of the denatureant with the protein surface.

TL;DR: Using a novel x-ray absolute-scale refinement method, this work determines the location, orientation, and likely conformation of monomeric melittin in oriented phosphocholine lipid multilayers and provides direct structural evidence that self-association of amphipathic helices may be the crucial initial step toward membrane lysis.

TL;DR: The marked tendency of the guanidinium ions to stack parallel to their water-deficient surfaces indicates that the efficiency of this ion as a denaturant is due to its ability to simultaneously interact favorably with both water and hydrophobic side chains of proteins.