TY - JOUR
T1 - In situ molecular level studies on membrane related peptides and proteins in real time using sum frequency generation vibrational spectroscopy
AU - Ye, Shuji
AU - Nguyen, Khoi Tan
AU - Clair, Stéphanie V.Le
AU - Chen, Zhan
N1 - Funding Information:
This research is supported by the National Institute of Health (1R01GM081655-01A2) and the Office of Naval Research (N00014-02-1-0832 and N00014-08-1-1211). SVLC acknowledges the Molecular Biophysics Training Grant from the University of Michigan.
PY - 2009/10
Y1 - 2009/10
N2 - Sum frequency generation (SFG) vibrational spectroscopy has been demonstrated to be a powerful technique to study the molecular structures of surfaces and interfaces in different chemical environments. This review summarizes recent SFG studies on hybrid bilayer membranes and substrate-supported lipid monolayers and bilayers, the interaction between peptides/proteins and lipid monolayers/bilayers, and bilayer perturbation induced by peptides/proteins. To demonstrate the ability of SFG to determine the orientations of various secondary structures, studies on the interactions between different peptides/proteins (melittin, G proteins, alamethicin, and tachyplesin I) and lipid bilayers are discussed. Molecular level details revealed by SFG in these studies show that SFG can provide a unique understanding on the interactions between a lipid monolayer/bilayer and peptides/proteins in real time, in situ and without any exogenous labeling.
AB - Sum frequency generation (SFG) vibrational spectroscopy has been demonstrated to be a powerful technique to study the molecular structures of surfaces and interfaces in different chemical environments. This review summarizes recent SFG studies on hybrid bilayer membranes and substrate-supported lipid monolayers and bilayers, the interaction between peptides/proteins and lipid monolayers/bilayers, and bilayer perturbation induced by peptides/proteins. To demonstrate the ability of SFG to determine the orientations of various secondary structures, studies on the interactions between different peptides/proteins (melittin, G proteins, alamethicin, and tachyplesin I) and lipid bilayers are discussed. Molecular level details revealed by SFG in these studies show that SFG can provide a unique understanding on the interactions between a lipid monolayer/bilayer and peptides/proteins in real time, in situ and without any exogenous labeling.
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U2 - 10.1016/j.jsb.2009.03.006
DO - 10.1016/j.jsb.2009.03.006
M3 - Article
C2 - 19306928
AN - SCOPUS:69249230898
SN - 1047-8477
VL - 168
SP - 61
EP - 77
JO - Journal of Structural Biology
JF - Journal of Structural Biology
IS - 1
ER -