Web Release Date: January 7,
Solid-State NMR Studies of the
Structure, Dynamics, and
Assembly of 
-Sheet Membrane
Peptides and 
-Helical
Membrane Proteins with
Antibiotic Activities
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.
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