ArticleBiophysical journal2008
FTIR spectroscopy of secondary-structure reorientation of melibiose permease modulated by substrate binding.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 28 citations in OpenAlex.
- Interaction of Lysozyme with Poly(L-lysine)/Hyaluronic Acid Multilayers: An ATR-FTIR Study.Polymers · 2023Article
- A photoswitchable helical peptide with light-controllable interface/transmembrane topology in lipidic membranes.iScience · 2021Article
- FTIR-based spectrum of salivary exosomes coupled with computational-aided discriminating analysis in the diagnosis of oral cancer.Journal of cancer research and clinical oncology · 2019Article
- Structural insights into the activation mechanism of melibiose permease by sodium binding.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Orientation and dynamics of transmembrane peptides: the power of simple models.European biophysics journal : EBJ · 2010Review
- Alteration of sugar-induced conformational changes of the melibiose permease by mutating Arg141 in loop 4-5.Biophysical journal · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Analysis of infrared polarized absorbance spectra and linear dichroism spectra of reconstituted melibiose permease from Escherichia coli shows that the oriented structures correspond mainly to tilted transmembrane alpha-helices, forming an average angle of approximately 26 degrees with the membrane normal in substrate-free medium. Examination of the deconvoluted linear dichroism spectra in H(2)O and D(2)O makes apparent two populations of alpha-helices differing by their tilt angle (helix types I and II). Moreover, the average helical tilt angle significantly varies upon substrate binding: it is increased upon Na(+) binding, whereas it decreases upon subsequent melibiose binding in the presence of Na(+). In contrast, melibiose binding in the presence of H(+) causes virtually no change in the average tilt angle. The data also suggest that the two helix populations change their tilting and H/D exchange level in different ways depending on the bound substrate(s). Notably, cation binding essentially influences type I helices, whereas melibiose binding modifies the tilting of both helix populations.
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