Solid-state NMR studies of the structure, dynamics, and assembly of beta-sheet membrane peptides and alpha-helical membrane proteins with antibiotic activities.
beta-Sheet antimicrobial peptides and alpha-helical channel-forming colicins are bactericidal molecules that target the lipid membranes of sensitive cells. Understanding the mechanisms of action of these proteins requires knowledge of their three-dimensional structure in the lipid bilayer. Solid-state NMR has been used to determine the conformation, orientation, depth of insertion, oligomerization, mobility, and lipid interaction of these membrane peptides and proteins. We review the NMR methods developed and applied to study the structure and dynamics of these antibiotic membrane proteins. These studies shed light on how these peptides disrupt lipid membranes and provide fundamental insights into the folding of beta-sheet and alpha-helical membrane proteins.
Hong
Mei
M
Department of Chemistry, Iowa State University, Ames, IA 50011, USA.
D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology; D001704:Biopolymers; D008051:Lipid Bilayers; D008565:Membrane Proteins / Q000737:chemistry* / Q000494:pharmacology; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology; D011487:Protein Conformation
D000900:Anti-Bacterial Agents; D001704:Biopolymers; D008051:Lipid Bilayers; D008565:Membrane Proteins; D010455:Peptides