ArticleBiophysical journal2004
A two-dimensional infrared study of localization, structure, and dynamics of a dipeptide in membrane environment.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed.
- Dynamics of Solvating Water As a Probe of Polymers and Supramolecular Structures.Chemical reviews · 2026Review
- Hydrogen-Bonded Complexes in Binary Mixture of Imidazolium-Based Ionic Liquids with Organic Solvents.The journal of physical chemistry. B · 2023Article
- Cu(Proline)Molecules (Basel, Switzerland) · 2022Article
- Disulfide bond influence on protein structural dynamics probed with 2D-IR vibrational echo spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Neuroglobin dynamics observed with ultrafast 2D-IR vibrational echo spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Electrostatic interactions in phospholipid membranes revealed by coherent 2D IR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Structural disorder of the CD3zeta transmembrane domain studied with 2D IR spectroscopy and molecular dynamics simulations.The journal of physical chemistry. B · 2006Article
- Amide vibrations are delocalized across the hydrophobic interface of a transmembrane helix dimer.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Two-dimensional infrared spectroscopy displays signatures of structural ordering in peptide aggregates.Biophysical journal · 2006Article
- Picosecond dynamics of a membrane protein revealed by 2D IR.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Probing the structure of a rotaxane with two-dimensional infrared spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
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2 authors.
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Abstract
Using methods of time-resolved two-dimensional infrared (2D-IR) spectroscopy, we approach the problem of the structural characterization of small polypeptide systems in a membrane environment. The 2D-IR spectra recorded for a model dipeptide in different environments demonstrated a significant change in the homogeneous and inhomogeneous broadenings of the amide I resonances when the molecule inserts either into a surfactant or a phospholipid membrane. Besides the change in the diagonal features in the 2D-IR response, we observe both intramolecular and intermolecular crosspeaks between the carbonyls of the dipeptide and the phospholipid. Considering the character of the diagonal peaks and the presence of the crosspeaks, we discuss the localization of the dipeptide moieties in the membrane. Using both the anisotropy and relative intensity of the observed intramolecular crosspeaks between the two amide I modes, we provide observables that help to determine the phi/psi-dihedral angles for the backbone of the dipeptide. Time dependent studies revealed slower conformational fluctuations of the dipeptide backbone in a membrane as compared to that in an aqueous environment.
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