Site-specific vibrational dynamics of the CD3zeta membrane peptide using heterodyned two-dimensional infrared photon echo spectroscopy

Heterodyned two-dimensional infrared (2D IR) spectroscopy has been used to study the amide I vibrational dynamics of a 27-residue peptide in lipid vesicles that encompasses the transmembrane domain of the T-cell receptor CD3zeta. Using 1-(13)C[Double Bond](18)O isotope labeling, the amide I mode of...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of chemical physics 2004-06, Vol.120 (21), p.10215-10224
Main Authors: Mukherjee, Prabuddha, Krummel, Amber T, Fulmer, Eric C, Kass, Itamar, Arkin, Isaiah T, Zanni, Martin T
Format: Article
Language:English
Subjects:
CD3 Complex - analysis
CD3 Complex - chemistry
Computer Simulation
Lipid Bilayers - chemistry
Liposomes - chemistry
Membrane Proteins - analysis
Membrane Proteins - chemistry
Models, Chemical
Models, Molecular
Peptides - analysis
Peptides - chemistry
Photons
Protein Conformation
Spectrophotometry, Infrared - methods
Vibration
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Heterodyned two-dimensional infrared (2D IR) spectroscopy has been used to study the amide I vibrational dynamics of a 27-residue peptide in lipid vesicles that encompasses the transmembrane domain of the T-cell receptor CD3zeta. Using 1-(13)C[Double Bond](18)O isotope labeling, the amide I mode of the 49-Leucine residue was spectroscopically isolated and the homogeneous and inhomogeneous linewidths of this mode were measured by fitting the 2D IR spectrum collected with a photon echo pulse sequence. The pure dephasing and inhomogeneous linewidths are 2 and 32 cm(-1), respectively. The population relaxation time of the amide I band was measured with a transient grating, and it contributes 9 cm(-1) to the linewidth. Comparison of the 49-Leucine amide I mode and the amide I band of the entire CD3zeta peptide reveals that the vibrational dynamics are not uniform along the length of the peptide. Possible origins for the large amount of inhomogeneity present at the 49-Leucine site are discussed.
ISSN:0021-9606