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

Mei Hong

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

Acc. Chem. Res., 2006, 39 (3), pp 176–183

DOI: 10.1021/ar040037e

Publication Date (Web): January 7, 2006

Mei Hong, Professor of Chemistry at Iowa State University, received her B.A. degree in 1992 from Mount Holyoke College and her Ph.D. in 1996 from the University of California, Berkeley. After one year of postdoctoral research at MIT, she became a Research Professor at the University of Massachusetts, Amherst, before joining Iowa State University in 1999. Her research focuses on the development and application of solid-state NMR methods to investigate the structure and dynamics of membrane proteins. For this, she received a number of awards, including a Beckman Young Investigator award, a NSF CAREER award, a Sloan Fellowship, and the American Chemical Society Pure Chemistry award.

Abstract

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

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Published In Issue March 21, 2006
Received October 3, 2005

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