Review: Mei Hong: Solid-State NMR of membrane proteins

Acc. Chem. Res., ASAP Article 10.1021/ar040037e S0001-4842(04)00037-8
Web Release Date: January 7, 2006

Solid-State NMR Studies of the Structure, Dynamics, and Assembly of -Sheet Membrane Peptides and -Helical Membrane Proteins with Antibiotic Activities

Mei Hong

Department of Chemistry, Iowa State University, Ames, Iowa 50011

Received October 3, 2005

Abstract:

-Sheet antimicrobial peptides and -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 -sheet and -helical membrane proteins.