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A New Method for Determining the Local Environment and Orientation of Individual Side Chains of Membrane-Binding Peptides
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Abstract

We studied here the binding of the mastoparan X peptide to a zwitterionic lipid bilayer (POPC) and demonstrated that nitrile-derivatized amino acids can be used to determine the hydration state (or change in hydration state) of specific sites of membrane-interactive peptides (upon binding). We have also shown that polarized ATR-FTIR measurements can further be used to uncover information regarding the spatial orientation of individual side chains as well as their conformational preference within the lipid bilayer.
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This article has been cited by 30 ACS Journal articles (5 most recent appear below).

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Computational Design of a β-Peptide That Targets Transmembrane Helices
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Direct Measurement of the Membrane Dipole Field in Bicelles Using Vibrational Stark Effect Spectroscopy
Wenhui Hu and Lauren J. WebbThe Journal of Physical Chemistry Letters2011 2 (15), 1925-1930Direct Measurement of the Membrane Dipole Field in Bicelles Using Vibrational Stark Effect Spectroscopy
Wenhui Hu and Lauren J. WebbThe Journal of Physical Chemistry Letters2011 2 (15), 1925-1930Electrostatic fields in lipid bilayer membranes influence the structure and function of membrane-associated proteins. We present here the first direct measurement of the membrane dipole electrostatic field in lipid bicelles using vibrational Stark effect ...
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History
- Published In Issue April 28, 2004
- Received December 31, 2003
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N stretching vibration in acetonitrile is sensitive to solvent. Therefore, we proposed in this contribution to use this vibrational mode to report local environment of a particular amino acid in proteins or local environmental ...
115 nm in diameter) were formed by dispersing polyaniline/formic acid solution into acetonitrile. It was demonstrated ...






