TY - CONF AU - Filep, Tibor AU - Zacháry, Dóra AU - Tőke, Orsolya AU - Domján, Attila AU - Szalai, Zoltán TI - Chemical differences in the non-protected carbon pool of four Hungarian soils with different vegetation types T2 - EGU General Assembly 2024 : abstracts PB - European Geosciences Union (EGU) C1 - Wien PY - 2024 DO - 10.5194/egusphere-egu24-8025 UR - https://m2.mtmt.hu/api/publication/34821191 ID - 34821191 N1 - poszter LA - English DB - MTMT ER - TY - JOUR AU - Tőke, Orsolya AU - Batta, Gyula TI - Dynamic Structures of Bioactive Proteins as Determined by Nuclear Magnetic Resonance JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 25 PY - 2024 IS - 1 PG - 6 SN - 1661-6596 DO - 10.3390/ijms25010295 UR - https://m2.mtmt.hu/api/publication/34510717 ID - 34510717 AB - According to “Panta rhei”, a phrase by the ancient Greeks, you cannot enter the same river two times [...] LA - English DB - MTMT ER - TY - JOUR AU - Miskolczy, Zsombor AU - Megyesi, Mónika AU - Turczel, Gábor AU - Tőke, Orsolya AU - Biczók, László TI - Substantial solubility and fluorescence property changes upon inclusion of rutaecarpine in cucurbit[7]uril: Kinetics and thermodynamics of binding JF - JOURNAL OF MOLECULAR LIQUIDS J2 - J MOL LIQ VL - 396 PY - 2024 PG - 9 SN - 0167-7322 DO - 10.1016/j.molliq.2024.124019 UR - https://m2.mtmt.hu/api/publication/34499234 ID - 34499234 N1 - Institute of Materials and Environmental Chemistry, HUN-REN Research Centre for Natural Sciences, P.O. Box 286, Budapest, 1519, Hungary NMR Research Laboratory, Centre for Structural Science, HUN-REN Research Centre for Natural Sciences, P.O. Box 286, Budapest, 1519, Hungary Export Date: 30 January 2024; Cited By: 0; Correspondence Address: L. Biczók; Institute of Materials and Environmental Chemistry, HUN-REN Research Centre for Natural Sciences, Budapest, P.O. Box 286, 1519, Hungary; email: biczok.laszlo@ttk.hu; CODEN: JMLID LA - English DB - MTMT ER - TY - JOUR AU - Tőke, Orsolya TI - Three Decades of REDOR in Protein Science: A Solid-State NMR Technique for Distance Measurement and Spectral Editing JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 24 PY - 2023 IS - 17 PG - 33 SN - 1661-6596 DO - 10.3390/ijms241713637 UR - https://m2.mtmt.hu/api/publication/34510707 ID - 34510707 AB - Solid-state NMR (ss-NMR) is a powerful tool to investigate noncrystallizable, poorly soluble molecular systems, such as membrane proteins, amyloids, and cell walls, in environments that closely resemble their physical sites of action. Rotational-echo double resonance (REDOR) is an ss-NMR methodology, which by reintroducing heteronuclear dipolar coupling under magic angle spinning conditions provides intramolecular and intermolecular distance restraints at the atomic level. In addition, REDOR can be exploited as a selection tool to filter spectra based on dipolar couplings. Used extensively as a spectroscopic ruler between isolated spins in site-specifically labeled systems and more recently as a building block in multidimensional ss-NMR pulse sequences allowing the simultaneous measurement of multiple distances, REDOR yields atomic-scale information on the structure and interaction of proteins. By extending REDOR to the determination of 1H–X dipolar couplings in recent years, the limit of measurable distances has reached ~15–20 Å, making it an attractive method of choice for the study of complex biomolecular assemblies. Following a methodological introduction including the most recent implementations, examples are discussed to illustrate the versatility of REDOR in the study of biological systems. LA - English DB - MTMT ER - TY - JOUR AU - Miskolczy, Zsombor AU - Megyesi, Mónika AU - Turczel, Gábor AU - Tőke, Orsolya AU - Biczók, László TI - Effect of inclusion in sulfobutylether-β-cyclodextrin on the rate of merocyanine-spirobenzopyran reversible photochromic transformations JF - DYES AND PIGMENTS J2 - DYES PIGMENTS VL - 219 PY - 2023 PG - 7 SN - 0143-7208 DO - 10.1016/j.dyepig.2023.111611 UR - https://m2.mtmt.hu/api/publication/34093500 ID - 34093500 N1 - Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, P.O. Box 286, Budapest, 1519, Hungary NMR Research Laboratory, Centre for Structural Science, Research Centre for Natural Sciences, P.O. Box 286, Budapest, 1519, Hungary Export Date: 25 August 2023; Cited By: 0; Correspondence Address: L. Biczók; Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, P.O. Box 286, 1519, Hungary; email: biczok.laszlo@ttk.hu; CODEN: DYPID LA - English DB - MTMT ER - TY - JOUR AU - Micsonai, András AU - Moussong, Éva AU - Murvai, Nikoletta AU - Tantos, Ágnes AU - Tőke, Orsolya AU - Réfrégiers, Matthieu AU - Wien, Frank AU - Kardos, József TI - Disordered-ordered protein binary classification by circular dichroism spectroscopy JF - BIOPHYSICAL JOURNAL J2 - BIOPHYS J VL - 122 PY - 2023 IS - 3 SP - 344a SN - 0006-3495 DO - 10.1016/j.bpj.2022.11.1915 UR - https://m2.mtmt.hu/api/publication/33660819 ID - 33660819 LA - English DB - MTMT ER - TY - JOUR AU - Horváth, Gergő AU - Balterer, Bence AU - Micsonai, András AU - Kardos, József AU - Tőke, Orsolya TI - Multiple Timescale Dynamic Analysis of Functionally-Impairing Mutations in Human Ileal Bile Acid-Binding Protein JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 23 PY - 2022 IS - 19 SN - 1661-6596 DO - 10.3390/ijms231911346 UR - https://m2.mtmt.hu/api/publication/33174847 ID - 33174847 N1 - NMR Research Laboratory, Centre for Structural Science, Research Centre for Natural Sciences, 2 Magyar Tudósok Körútja, Budapest, H-1117, Hungary ELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Pázmány Péter sétány 1/C, Budapest, H-1117, Hungary Export Date: 21 November 2022 Correspondence Address: Toke, O.; NMR Research Laboratory, 2 Magyar Tudósok Körútja, Hungary; email: toke.orsolya@ttk.hu AB - Human ileal bile acid-binding protein (hI-BABP) has a key role in the enterohepatic circulation of bile salts. Its two internal binding sites exhibit positive cooperativity accompanied by a site-selectivity of glycocholate (GCA) and glycochenodeoxycholate (GCDA), the two most abundant bile salts in humans. To improve our understanding of the role of dynamics in ligand binding, we introduced functionally impairing single-residue mutations at two key regions of the protein and subjected the mutants to NMR relaxation analysis and MD simulations. According to our results, mutation in both the vicinity of the C/D (Q51A) and the G/H (Q99A) turns results in a redistribution of motional freedom in apo hI-BABP. Mutation Q51A, deteriorating the site-selectivity of GCA and GCDA, results in the channeling of ms fluctuations into faster motions in the binding pocket hampering the realization of key side chain interactions. Mutation Q99A, abolishing positive binding cooperativity for GCDA, leaves ms motions in the C-terminal half unchanged but by decoupling βD from a dynamic cluster of the N-terminal half displays an increased flexibility in the vicinity of site 1. MD simulations of the variants indicate structural differences in the portal region and mutation-induced changes in dynamics, which depend on the protonation state of histidines. A dynamic coupling between the EFGH portal, the C/D-region, and the helical cap is evidenced highlighting the interplay of structural and dynamic effects in bile salt recognition in hI-BABP. LA - English DB - MTMT ER - TY - JOUR AU - Pálfy, Gyula AU - Karancsiné Menyhárd, Dóra AU - Ákontz-Kiss, Hanna AU - Vida, István AU - Batta, Gyula AU - Tőke, Orsolya AU - Perczel, András TI - The Importance of Mg2+‐free State in Nucleotide Exchange of Oncogenic K‐Ras Mutants JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 28 PY - 2022 IS - 59 PG - 14 SN - 0947-6539 DO - 10.1002/chem.202201449 UR - https://m2.mtmt.hu/api/publication/32924494 ID - 32924494 N1 - Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, 1/a Pázmány Péter stny., Budapest, 1117, Hungary MTA-ELTE Protein Modeling Research Group, Eötvös Loránd Research Network (ELKH), 1/a Pázmány Péter stny., Budapest, 1117, Hungary Hevesy György PhD School of Chemistry, Eötvös Loránd University, 1/a Pázmány Péter stny., Budapest, 1117, Hungary Structural Biology Research Group, Department of Organic Chemistry, University of Debrecen, 1 Egyetem tér, Debrecen, 4032, Hungary Laboratory for NMR Spectroscopy, Research Centre for Natural Sciences (RCNS), 2 Magyar tudósok körútja, Budapest, 1117, Hungary Cited By :3 Export Date: 6 April 2023 CODEN: CEUJE Correspondence Address: Perczel, A.; Laboratory of Structural Chemistry and Biology, 1/a Pázmány Péter stny., Hungary; email: perczel.andras@ttk.elte.hu AB - For efficient targeting of oncogenic K-Ras interaction sites, a mechanistic picture of the Ras-cycle is necessary. Herein, we used NMR relaxation techniques and molecular dynamics simulations to decipher the role of slow dynamics in wild-type and three oncogenic P-loop mutants of K-Ras. Our measurements reveal a dominant two-state conformational exchange on the ms timescale in both GDP- and GTP-bound KRas. The identified low-populated higher energy state in GDPloaded K-Ras has a conformation reminiscent of a nucleotidebound/Mg2+-free state characterized by shortened β2/β3-strands and a partially released switch-I region preparing K-Ras for the interaction with the incoming nucleotide exchange factor and subsequent reactivation. By providing insight into mutationspecific differences in K-Ras structural dynamics, our systematic analysis improves our understanding of prolonged K-Ras signaling and may aid the development of allosteric inhibitors targeting nucleotide exchange in K-Ras. LA - English DB - MTMT ER - TY - JOUR AU - Micsonai, András AU - Moussong, Éva AU - Murvai, Nikoletta AU - Tantos, Ágnes AU - Tőke, Orsolya AU - Réfrégiers, Matthieu AU - Wien, Frank AU - Kardos, József TI - Disordered–Ordered Protein Binary Classification by Circular Dichroism Spectroscopy JF - FRONTIERS IN MOLECULAR BIOSCIENCES J2 - FRONT MOL BIOSCI VL - 9 PY - 2022 PG - 10 SN - 2296-889X DO - 10.3389/fmolb.2022.863141 UR - https://m2.mtmt.hu/api/publication/32819946 ID - 32819946 N1 - ELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary Institute of Enzymology, Research Centre for Natural Sciences, Budapest, Hungary Laboratory for NMR Spectroscopy, Research Centre for Natural Sciences, Budapest, Hungary Synchrotron SOLEIL, Gif-sur-Yvette, France Centre de Biophysique Moléculaire, CNRS UPR4301, Orléans, France Cited By :2 Export Date: 22 August 2022 Correspondence Address: Kardos, J.; ELTE NAP Neuroimmunology Research Group, Hungary; email: kardos@elte.hu LA - English DB - MTMT ER - TY - JOUR AU - Tőke, Orsolya TI - Structural and Dynamic Determinants of Molecular Recognition in Bile Acid-Binding Proteins JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 23 PY - 2022 IS - 1 SN - 1661-6596 DO - 10.3390/ijms23010505 UR - https://m2.mtmt.hu/api/publication/32590583 ID - 32590583 LA - English DB - MTMT ER -