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653 results on '"Goormaghtigh, Erik"'

8. Structures of intermediate transport states of ZneA, a Zn(II)/proton antiporter

Author

Pak, John Edward, Ekendé, Elisabeth Ngonlong, Kifle, Efrem G, O’Connell, Joseph Daniel, De Angelis, Fabien, Tessema, Meseret B, Derfoufi, Kheiro-Mouna, Robles-Colmenares, Yaneth, Robbins, Rebecca A, Goormaghtigh, Erik, Vandenbussche, Guy, and Stroud, Robert M

Subjects
Antimicrobial Resistance, Emerging Infectious Diseases, Infectious Diseases, Generic health relevance, Antiporters, Bacterial Proteins, Biological Transport, Crystallization, Cupriavidus, Models, Molecular, Protein Conformation, Protons, X-Ray Diffraction, Zinc
Abstract

Efflux pumps belonging to the ubiquitous resistance-nodulation-cell division (RND) superfamily transport substrates out of cells by coupling proton conduction across the membrane to a conformationally driven pumping cycle. The heavy metal-resistant bacteria Cupriavidus metallidurans CH34 relies notably on as many as 12 heavy metal efflux pumps of the RND superfamily. Here we show that C. metallidurans CH34 ZneA is a proton driven efflux pump specific for Zn(II), and that transport of substrates through the transmembrane domain may be electrogenic. We report two X-ray crystal structures of ZneA in intermediate transport conformations, at 3.0 and 3.7 Å resolution. The trimeric ZneA structures capture protomer conformations that differ in the spatial arrangement and Zn(II) occupancies at a proximal and a distal substrate binding site. Structural comparison shows that transport of substrates through a tunnel that links the two binding sites, toward an exit portal, is mediated by the conformation of a short 14-aa loop. Taken together, the ZneA structures presented here provide mechanistic insights into the conformational changes required for substrate efflux by RND superfamily transporters.

Published
2013

20. FTIR spectroscopy as a multi-parameter analytical tool: FTIR can successfully measure key characteristics of therapeutic proteins in a single step

Author

Derenne, Allison and Goormaghtigh, Erik

Subjects
Biopharmaceuticals -- Health aspects, Proteins -- Health aspects, Infrared spectroscopy -- Health aspects, Biotechnology industry, Business, Pharmaceuticals and cosmetics industries
Abstract

Rapid commercialization of therapeutic proteins remains a challenge notably due to their chemical and physical instabilities. Yet, the inherent complexity of proteins requires the development of new analytical strategies to [...]

Published
2017

27. A new alternative tool to analyse glycosylation in pharmaceutical proteins based on infrared spectroscopy combined with nonlinear support vector regression

Author

Hamla, Sabrina, primary, Sacré, Pierre-Yves, additional, Derenne, Allison, additional, Derfoufi, Kheiro-Mouna, additional, Cowper, Ben, additional, Butré, Claire I., additional, Delobel, Arnaud, additional, Goormaghtigh, Erik, additional, Hubert, Philippe, additional, and Ziemons, Eric, additional

Published
2022
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34. Analysis of Glycoproteins by ATR-FTIR Spectroscopy: Comparative Assessment

Author

Derenne, Allison, Derfoufi, Kheiro-Mouna, Cowper, Ben, Delporte, Cédric, Butré, Claire CI, and Goormaghtigh, Erik

Subjects
Glycosylation, Time Factors, technology, industry, and agriculture, macromolecular substances, Sciences bio-médicales et agricoles, Mass Spectrometry, Workflow, FTIR spectroscopy, stomatognathic system, Research Design, Spectroscopy, Fourier Transform Infrared, Glycoproteins -- analysis, lipids (amino acids, peptides, and proteins), Monoclonal antibodies, Antibodies, Monoclonal -- analysis, Infrared, Protein Processing, Post-Translational, Glycoproteins, biosimilar
Abstract

FTIR spectroscopy has been widely used to characterize biopharmaceuticals for many years, in particular to analyze protein structure. More recently, it was demonstrated to be a useful tool to study and compare protein samples in terms of glycosylation. Based on a spectral region specific to carbohydrate absorption, we present here a detailed protocol to compare the FTIR spectra of glycoproteins in terms of global glycosylation level and in terms of glycan composition. This FTIR information is compared to MS information. Both approaches yield consistent results but it appears FTIR analysis is easier and more rapid to perform comparisons., info:eu-repo/semantics/published

Published
2021

42. Modulation of the membrane orientation and secondary structure of the C-terminal domains of Bak and Bcl-2 by lipids

Author

Torrecillas, Alejandro, Goormaghtigh, Erik, Godos, Ana de, Martinez-Senac, Maria M., and Corbalan-Garcia, Senena

Subjects
Infrared spectroscopy -- Research, Amino acid sequence -- Research, Membrane proteins -- Research, Biological sciences, Chemistry
Abstract

Infrared spectroscopy was used to study the secondary structure of peptides, which imitate the amino acid sequences of the C-terminal domains of the pro-apoptotic Bak, and anti-apoptotic Bcl-2 proteins when they are inserted in lipid vesicles. It was concluded that the domains only form transmembrane helices in membranes of reduced thickness and that hydrophobic mismatching occurs in thicker membranes.

Published
2005

46. Structure and dynamics of the membrane-embedded domain of LmrA investigated by coupling polarized ATR-FTIR spectroscopy and (super)1 H/ (super)2 H exchange

Author

Grimard, Vinciane, Vigano, Catherine, Margolles, Abelardo, Wattiez, Ruddy, Veen, Hendrik W. van, Konings, Wil N., Ruysschaert, Jean-Marie, and Goormaghtigh, Erik

Subjects
Biochemistry -- Research, Hydrogen -- Physiological aspects, Fourier transform infrared spectroscopy -- Usage, Membrane proteins -- Analysis, Infrared spectroscopy -- Usage, Lactococcus -- Physiological aspects, Proteolysis -- Analysis, Biological sciences, Chemistry
Abstract

Research has been conducted on the bacterial LmrA, Lactococcus lactis's integral membrane protein. The secondary structure and the orientation of the LmrA's transmembrane segments have been investigated via the polarized attenuated total reflection infrared spectroscopy and limited proteolysis.

Published
2001

47. Sensitivity of single membrane-spanning alpha-helical peptides to hydrophobic mismatch with a lipid bilayer: effects on backbone structure, orientation, and extent of membrane incorporation

Author

Planque, Maurits R.R. de, Goormaghtigh, Erik, Greathouse, Denise V., Koeppe, Roger E., II, Kruijtzer, John A.W., Liskamp, Rob M.J., Kruijff, Ben de, and Killian, J. Antoinette

Subjects
Bilayer lipid membranes -- Research, Membrane proteins -- Research, Biological sciences, Chemistry
Abstract

The extent of incorporation of membrane proteins is reduced when there is a hydrophobic mismatch between membrane lipids and membrane proteins. As the mismatch increases, smaller amounts of the protein are incorporated into the lipid bilayer and larger amounts are found outside the membrane.

Published
2001

48. Conformational changes of the 120-kDa Na(sup)+/Ca(sup)2+ exchange protein upon ligand binding: a Fourier transform infrared spectroscopy study

Author

Saba, Rami I., Goormaghtigh, Erik, Jean-Marie Ruysschaert, and Herchuelz, Andre

Subjects
Conformational analysis -- Research, Proteins -- Conformation, Ligand binding (Biochemistry) -- Analysis, Fourier transform infrared spectroscopy -- Usage, Biological sciences, Chemistry
Abstract

Results demonstrate that binding of calcium activator and XIP inhibitory peptide to the sodium/calcium exchanger protein produces conformational changes. Data suggest that the activator and the inhibitor bind to distinct sites.

Published
2001

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