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Structure and dynamics of cationic membrane peptides and proteins: Insights from solid‐state NMR
Author(s) -
Hong Mei,
Su Yongchao
Publication year - 2011
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.600
Subject(s) - lipid bilayer , chemistry , cationic polymerization , membrane , nuclear magnetic resonance spectroscopy , membrane protein , peripheral membrane protein , solid state nuclear magnetic resonance , molecular dynamics , helix (gastropod) , biophysics , crystallography , stereochemistry , integral membrane protein , biochemistry , computational chemistry , biology , organic chemistry , ecology , physics , nuclear magnetic resonance , snail
Abstract Many membrane peptides and protein domains contain functionally important cationic Arg and Lys residues, whose insertion into the hydrophobic interior of the lipid bilayer encounters significant energy barriers. To understand how these cationic molecules overcome the free energy barrier to insert into the lipid membrane, we have used solid‐state NMR spectroscopy to determine the membrane‐bound topology of these peptides. A versatile array of solid‐state NMR experiments now readily yields the conformation, dynamics, orientation, depth of insertion, and site‐specific protein–lipid interactions of these molecules. We summarize key findings of several Arg‐rich membrane peptides, including β‐sheet antimicrobial peptides, unstructured cell‐penetrating peptides, and the voltage‐sensing helix of voltage‐gated potassium channels. Our results indicate the central role of guanidinium‐phosphate and guanidinium‐water interactions in dictating the structural topology of these cationic molecules in the lipid membrane, which in turn account for the mechanisms of this functionally diverse class of membrane peptides.