Výsledky vyhledávání - "Triple-resonance nuclear magnetic resonance spectroscopy"

Minimizing Pervasive Artifacts in 4D Covariance Maps for Protein Side Chain NMR Assignments

Autor: Dominique P. Frueh, Aswani K. Kancherla, Subrata H. Mishra, Kenneth A. Marincin

Publikováno v: J Phys Chem A

[Image: see text] Nuclear magnetic resonance (NMR) is a mainstay of biophysical studies that provides atomic level readouts to formulate molecular mechanisms. Side chains are particularly important to derive mechanisms involving proteins as they carr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90b972043a6b31a0929e0903be191b4e
https://doi.org/10.1021/acs.jpca.1c05507

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Triple Resonance Experiments for the Rapid Detection of 103Rh NMR Shifts: A Combined Experimental and Theoretical Study into Dirhodium and Bismuth–Rhodium Paddlewheel Complexes

Autor: Alois Fürstner, Giovanni Bistoni, Markus Leutzsch, Fabio P. Caló, Alexander A. Auer

Publikováno v: Journal of the American Chemical Society

A H(C)Rh triple resonance NMR experiment makes the rapid detection of 103Rh chemical shifts possible, which were previously beyond reach. It served to analyze a series of dirhodium and bismuth-rhodium paddlewheel complexes of the utmost importance fo

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http://europepmc.org/articles/PMC8377716

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NMR Spectroscopy in the Conformational Analysis of Peptides: An Overview

Autor: Marilisa Leone, Flavia Anna Mercurio, Marian Vincenzi

Publikováno v: Current medicinal chemistry (2020). doi:10.2174/0929867327666200702131032
info:cnr-pdr/source/autori:Vincenzi M, Mercurio FA, Leone M./titolo:NMR spectroscopy in the conformational analysis of peptides: an overview./doi:10.2174%2F0929867327666200702131032/rivista:Current medicinal chemistry/anno:2020/pagina_da:/pagina_a:/intervallo_pagine:/volume

Background: NMR spectroscopy is one of the most powerful tools to study the structure and interaction properties of peptides and proteins from a dynamic perspective. Knowing the bioactive conformations of peptides is crucial in the drug discovery fie

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https://doi.org/10.2174/0929867327666200702131032

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NMR mapping of the highly flexible regions of 13C/15N-labeled antibody TTAC-0001-Fab

Autor: Jin-San Yoo, Kyoung-Seok Ryu, Jong Geun Jeong, Soyoung Cha, Joonhyeok Choi, Joon-Hwa Lee, Jihong Kim, Ju Ryoung Nam, Hak-Nam Kim, Weon Sup Lee

Publikováno v: Journal of Biomolecular NMR. 74:311-319

Monoclonal antibody (mAb) drugs are clinically important for the treatment of various diseases. TTAC-0001 is under development as a new anti-cancer antibody drug targeting VEGFR-2. As the less severe toxicity of TTAC-0001 compared to Bevacizumab, lik

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https://doi.org/10.1007/s10858-020-00313-1

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1H, 13C and 15N assignment of the paramagnetic high potential iron–sulfur protein (HiPIP) PioC from Rhodopseudomonas palustris TIE-1

Autor: Inês B. Trindade, Francesca Cantini, Ricardo O. Louro, Mario Piccioli, Michele Invernici

Publikováno v: Biomolecular Nmr Assignments

High potential iron–sulfur proteins (HiPIPs) are a class of small proteins (50–100 aa residues), containing a 4Fe–4S iron–sulfur cluster. The 4Fe–4S cluster shuttles between the oxidation states [Fe4S4]3+/2+, with a positive redox potential

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http://europepmc.org/articles/PMC7462912

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1H, 13C, 15N backbone NMR resonance assignments for the rRNA methyltransferase Dim1 from the hyperthermophilic archaeon Pyrococcus horikoshii

Autor: Carolin Hacker, Marco Kaiser, Jens Wöhnert, Elke Duchardt-Ferner

Publikováno v: Biomolecular NMR Assignments. 13:309-314

The protein dimethyladenosine transferase 1 (Dim1) is a highly conserved protein occurring in organisms ranging from bacteria such as E. coli where it is named KsgA to humans. Since Dim1 is involved in the biogenesis of the small ribosomal subunit it

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https://doi.org/10.1007/s12104-019-09897-8

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NMR resonance assignments for the GTP-binding RNA aptamer 9-12 in complex with GTP

Autor: Robbin Schnieders, Jens Wöhnert, Antje C. Wolter, Elisabeth Strebitzer, Elke Duchardt-Ferner, Angela Pianu, Boris Fürtig, Christoph Kreutz, Johannes Kremser

Publikováno v: Biomolecular NMR Assignments. 13:281-286

Ligand binding RNAs such as artificially created RNA-aptamers are structurally highly diverse. Therefore, they represent important model systems for investigating RNA-folding, RNA-dynamics and the molecular recognition of chemically very different li

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https://doi.org/10.1007/s12104-019-09892-z

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NMR resonance assignments for the SAM/SAH-binding riboswitch RNA bound to S-adenosylhomocysteine

Autor: Heiko Keller, Jens Wöhnert, Michael Andreas Juen, Christoph Kreutz, Elke Duchardt-Ferner, Elisabeth Strebitzer, Johannes Kremser, Jan Philip Wurm, A. Katharina Weickhmann

Publikováno v: Biomolecular NMR Assignments. 12:329-334

Riboswitches are structured RNA elements in the 5'-untranslated regions of bacterial mRNAs that are able to control the transcription or translation of these mRNAs in response to the specific binding of small molecules such as certain metabolites. Ri

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https://doi.org/10.1007/s12104-018-9834-3

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Heteronuclear transfers from labile protons in biomolecular NMR: Cross polarization, revisited

Autor: Jihyun Kim, Adonis Lupulescu, Maria Grazia Concilio, S. Jayanthi, Mihajlo Novakovic, Lucio Frydman, David Columbus, Ilya Kuprov

Publikováno v: Journal of Magnetic Resonance

INEPT- and HMQC-based pulse sequences are widely used to transfer polarization between heteronuclei, particularly in biomolecular spectroscopy: they are easy to setup and involve low power deposition. Still, these short-pulse polarization transfers s

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https://doi.org/10.1016/j.jmr.2021.107083

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Optimization of 1H decoupling eliminates sideband artifacts in 3D TROSY-based triple resonance experiments

Autor: Charalampos G. Kalodimos, Marco Tonelli, Chengdong Huang, Paolo Rossi, Youlin Xia, Gianluigi Veglia

Publikováno v: Journal of Biomolecular NMR. 69:45-52

TROSY-based triple resonance experiments are essential for protein backbone assignment of large biomolecular systems by solution NMR spectroscopy. In a survey of the current Bruker pulse sequence library for TROSY-based experiments we found that seve

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60482b4c1316acc1cbe67d801dfde829
https://doi.org/10.1007/s10858-017-0133-6

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