Site-specific vibrational dynamics of the CD3ζ 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 CD3ζ. Using 1–13C=18O isotope labeling, the amide I mode of the 49-Leucine resi...
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Veröffentlicht in: | The Journal of chemical physics 2004-06, Vol.120 (21), p.10215-10224 |
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Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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 CD3ζ. Using 1–13C=18O 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 CD3ζ 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. |
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ISSN: | 0021-9606 1089-7690 |
DOI: | 10.1063/1.1718332 |