Unknown

Dataset Information

0

In situ molecular level studies on membrane related peptides and proteins in real time using sum frequency generation vibrational spectroscopy.


ABSTRACT: 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.

SUBMITTER: Ye S 

PROVIDER: S-EPMC2753614 | biostudies-other | 2009 Oct

REPOSITORIES: biostudies-other

altmetric image

Publications

In situ molecular level studies on membrane related peptides and proteins in real time using sum frequency generation vibrational spectroscopy.

Ye Shuji S   Nguyen Khoi Tan KT   Le Clair Stéphanie V SV   Chen Zhan Z  

Journal of structural biology 20090321 1


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 determin  ...[more]

Similar Datasets

| S-EPMC1913150 | biostudies-literature
| S-EPMC555967 | biostudies-literature
| S-EPMC4516311 | biostudies-other
| S-EPMC3910618 | biostudies-literature
| S-EPMC5444077 | biostudies-literature
| S-EPMC4434775 | biostudies-literature
| S-EPMC3122884 | biostudies-literature
| S-EPMC5647563 | biostudies-literature
| S-EPMC3128200 | biostudies-literature
| S-EPMC5924933 | biostudies-literature