-
Fluorine-19 labeling of the tryptophan residues in the G protein-coupled receptor NK1R using the 5-fluoroindole precursor in Pichia pastoris expression J. Biomol. NMR (IF 2.7) Pub Date : 2024-03-30 Benxun Pan, Canyong Guo, Dongsheng Liu, Kurt Wüthrich
In NMR spectroscopy of biomolecular systems, the use of fluorine-19 probes benefits from a clean background and high sensitivity. Therefore, 19F-labeling procedures are of wide-spread interest. Here, we use 5-fluoroindole as a precursor for cost-effective residue-specific introduction of 5-fluorotryptophan (5F-Trp) into G protein-coupled receptors (GPCRs) expressed in Pichia pastoris. The method was
-
Enabling site-specific NMR investigations of therapeutic Fab using a cell-free based isotopic labeling approach: application to anti-LAMP1 Fab J. Biomol. NMR (IF 2.7) Pub Date : 2024-03-28 Arthur Giraud, Lionel Imbert, Adrien Favier, Faustine Henot, Francis Duffieux, Camille Samson, Oriane Frances, Elodie Crublet, Jérôme Boisbouvier
-
Prediction of order parameters based on protein NMR structure ensemble and machine learning J. Biomol. NMR (IF 2.7) Pub Date : 2024-03-26 Qianqian Wang, Zhiwei Miao, Xiongjie Xiao, Xu Zhang, Daiwen Yang, Bin Jiang, Maili Liu
-
DNP-assisted solid-state NMR enables detection of proteins at nanomolar concentrations in fully protonated cellular milieu J. Biomol. NMR (IF 2.7) Pub Date : 2024-03-23 Whitney N. Costello, Yiling Xiao, Frederic Mentink-Vigier, Jaka Kragelj, Kendra K. Frederick
-
Decorating phenylalanine side-chains with triple labeled 13C/19F/2H isotope patterns J. Biomol. NMR (IF 2.7) Pub Date : 2024-03-21 Giorgia Toscano, Julian Holzinger, Benjamin Nagl, Georg Kontaxis, Hanspeter Kählig, Robert Konrat, Roman J. Lichtenecker
-
Reconstitution and resonance assignments of yeast OST subunit Ost4 and its critical mutant Ost4V23D in liposomes by solid-state NMR J. Biomol. NMR (IF 2.7) Pub Date : 2024-02-29 Bharat P. Chaudhary, Jochem Struppe, Hem Moktan, David Zoetewey, Donghua H. Zhou, Smita Mohanty
-
Fluorine labelling for in situ 19F NMR in oriented systems J. Biomol. NMR (IF 2.7) Pub Date : 2024-02-26 Kieran T. Cockburn, Brian D. Sykes
-
A comprehensive assessment of selective amino acid 15N-labeling in human embryonic kidney 293 cells for NMR spectroscopy J. Biomol. NMR (IF 2.7) Pub Date : 2024-02-26 Ganesh P. Subedi, Elijah T. Roberts, Alexander R. Davis, Paul G. Kremer, I. Jonathan Amster, Adam W. Barb
-
Beyond slow two-state protein conformational exchange using CEST: applications to three-state protein interconversion on the millisecond timescale J. Biomol. NMR (IF 2.7) Pub Date : 2024-01-03 Ved Prakash Tiwari, Debajyoti De, Nemika Thapliyal, Lewis E. Kay, Pramodh Vallurupalli
-
The NMR signature of maltose-based glycation in full-length proteins J. Biomol. NMR (IF 2.7) Pub Date : 2023-12-20 Pauline Defant, Christof Regl, Christian G. Huber, Mario Schubert
Reducing sugars can spontaneously react with free amines in protein side chains leading to posttranslational modifications (PTMs) called glycation. In contrast to glycosylation, glycation is a non-enzymatic modification with consequences on the overall charge, solubility, aggregation susceptibility and functionality of a protein. Glycation is a critical quality attribute of therapeutic monoclonal antibodies
-
Short and long range 2D 15N–15N NMR correlations among peptide groups by novel solid state dipolar mixing schemes J. Biomol. NMR (IF 2.7) Pub Date : 2023-12-16 Sungsool Wi, Conggang Li, Karen Pham, Woonghee Lee, Lucio Frydman
-
Uniform [13C,15N]-labeled and glycosylated IgG1 Fc expressed in Saccharomyces cerevisiae J. Biomol. NMR (IF 2.7) Pub Date : 2023-11-21 Alexander R. Davis, Elijah T. Roberts, I. Jonathan Amster, Adam W. Barb
-
Efficient determination of the accessible conformation space of multi-domain complexes based on EPR PELDOR data J. Biomol. NMR (IF 2.7) Pub Date : 2023-11-15 Sina Kazemi, Anna Lopata, Andreas Kniss, Lukas Pluska, Peter Güntert, Thomas Sommer, Thomas F. Prisner, Alberto Collauto, Volker Dötsch
-
5D solid-state NMR spectroscopy for facilitated resonance assignment J. Biomol. NMR (IF 2.7) Pub Date : 2023-11-09 Alexander Klein, Suresh K. Vasa, Rasmus Linser
-
Paramagnetic NMR to study iron sulfur proteins: 13C detected experiments illuminate the vicinity of the metal center J. Biomol. NMR (IF 2.7) Pub Date : 2023-10-18 Leonardo Querci, Deborah Grifagni, Inês B. Trindade, José Malanho Silva, Ricardo O. Louro, Francesca Cantini, Mario Piccioli
-
Synthesis of a 13C-methylene-labeled isoleucine precursor as a useful tool for studying protein side-chain interactions and dynamics J. Biomol. NMR (IF 2.7) Pub Date : 2023-10-11 Theresa Höfurthner, Giorgia Toscano, Georg Kontaxis, Andreas Beier, Moriz Mayer, Leonhard Geist, Darryl B. McConnell, Harald Weinstabl, Roman Lichtenecker, Robert Konrat
-
Breaking boundaries: TINTO in POKY for computer vision-based NMR walking strategies J. Biomol. NMR (IF 2.7) Pub Date : 2023-10-07 Andrea Estefania Lopez Giraldo, Zowie Werner, Mehdi Rahimi, Woonghee Lee
-
A thermosensitive gel matrix for bioreactor-assisted in-cell NMR of nucleic acids and proteins J. Biomol. NMR (IF 2.7) Pub Date : 2023-09-09 Matej Dzurov, Šárka Pospíšilová, Michaela Krafčíková, Lukáš Trantírek, Lucy Vojtová, Jan Ryneš
-
Strategies for acquisition of resonance assignment spectra of highly dynamic membrane proteins: a GPCR case study J. Biomol. NMR (IF 2.7) Pub Date : 2023-07-26 Evan J. van Aalst, Jun Jang, Ty C. Halligan, Benjamin J. Wylie
-
Improved spectral resolution of [13C,1H]-HSQC spectra of aromatic amino acid residues in proteins produced by cell-free synthesis from inexpensive 13C-labelled precursors J. Biomol. NMR (IF 2.7) Pub Date : 2023-06-20 Damian Van Raad, Thomas Huber, Gottfried Otting
-
E. coli “Stablelabel” S30 lysate for optimized cell-free NMR sample preparation J. Biomol. NMR (IF 2.7) Pub Date : 2023-06-13 Roman Levin, Frank Löhr, Betül Karakoc, Roman Lichtenecker, Volker Dötsch, Frank Bernhard
-
Studying micro to millisecond protein dynamics using simple amide 15N CEST experiments supplemented with major-state R2 and visible peak-position constraints J. Biomol. NMR (IF 2.7) Pub Date : 2023-06-10 Nihar Pradeep Khandave, Ashok Sekhar, Pramodh Vallurupalli
-
Efficient 18.8 T MAS-DNP NMR reveals hidden side chains in amyloid fibrils J. Biomol. NMR (IF 2.7) Pub Date : 2023-06-08 Alons Lends, Nicolas Birlirakis, Xinyi Cai, Asen Daskalov, Jayakrishna Shenoy, Muhammed Bilal Abdul-Shukkoor, Mélanie Berbon, Fabien Ferrage, Yangping Liu, Antoine Loquet, Kong Ooi Tan
-
1H-detected characterization of carbon–carbon networks in highly flexible protonated biomolecules using MAS NMR J. Biomol. NMR (IF 2.7) Pub Date : 2023-06-08 Salima Bahri, Adil Safeer, Agnes Adler, Hanneke Smedes, Hugo van Ingen, Marc Baldus
-
Non-uniform sampling of similar NMR spectra and its application to studies of the interaction between alpha-synuclein and liposomes J. Biomol. NMR (IF 2.7) Pub Date : 2023-05-26 Alexandra Shchukina, Thomas C. Schwarz, Michał Nowakowski, Robert Konrat, Krzysztof Kazimierczuk
-
A methyl-TROSY based 13C relaxation dispersion NMR experiment for studies of chemical exchange in proteins J. Biomol. NMR (IF 2.7) Pub Date : 2023-04-25 Vitali Tugarinov, James L. Baber, G. Marius Clore
-
NMR detection and conformational dependence of two, three, and four-bond isotope shifts due to deuteration of backbone amides J. Biomol. NMR (IF 2.7) Pub Date : 2023-04-24 Andrei T. Alexandrescu, Aurelio J. Dregni, Carolyn M. Teschke
-
Sparse pseudocontact shift NMR data obtained from a non-canonical amino acid-linked lanthanide tag improves integral membrane protein structure prediction J. Biomol. NMR (IF 2.7) Pub Date : 2023-04-04 Kaitlyn V. Ledwitch, Georg Künze, Jacob R. McKinney, Elleansar Okwei, Katherine Larochelle, Lisa Pankewitz, Soumya Ganguly, Heather L. Darling, Irene Coin, Jens Meiler
-
Assessing the applicability of 19F labeled tryptophan residues to quantify protein dynamics J. Biomol. NMR (IF 2.7) Pub Date : 2023-01-14 Christina Krempl, Remco Sprangers
-
Three segment ligation of a 104 kDa multi-domain protein by SrtA and OaAEP1 J. Biomol. NMR (IF 2.7) Pub Date : 2022-12-21 Stephan B. Azatian, Marella D. Canny, Michael P. Latham
-
Water irradiation devoid pulses enhance the sensitivity of 1H,1H nuclear Overhauser effects J. Biomol. NMR (IF 2.7) Pub Date : 2022-12-19 V. S. Manu, Cristina Olivieri, Gianluigi Veglia
-
Efficiently driving protein-based fragment screening and lead discovery using two-dimensional NMR J. Biomol. NMR (IF 2.7) Pub Date : 2022-12-13 Chen Peng, Andrew T. Namanja, Eva Munoz, Haihong Wu, Thomas E. Frederick, Mitcheell Maestre-Martinez, Isaac Iglesias Fernandez, Qi Sun, Carlos Cobas, Chaohong Sun, Andrew M. Petros
-
Investigation of lipid/protein interactions in trifluoroethanol-water mixtures proposes the strategy for the refolding of helical transmembrane domains J. Biomol. NMR (IF 2.7) Pub Date : 2022-11-30 Vladislav V. Motov, Erik F. Kot, Alexandra V. Shabalkina, Sergey A. Goncharuk, Alexander S. Arseniev, Marina V. Goncharuk, Konstantin S. Mineev
-
Band-selective universal 90° and 180° rotation pulses covering the aliphatic carbon chemical shift range for triple resonance experiments on 1.2 GHz spectrometers J. Biomol. NMR (IF 2.7) Pub Date : 2022-11-24 Stella Slad, Wolfgang Bermel, Rainer Kümmerle, Daniel Mathieu, Burkhard Luy
-
Pure shift amide detection in conventional and TROSY-type experiments of 13C,15N-labeled proteins J. Biomol. NMR (IF 2.7) Pub Date : 2022-11-18 Jens D. Haller, Andrea Bodor, Burkhard Luy
-
Optimizing frequency sampling in CEST experiments J. Biomol. NMR (IF 2.7) Pub Date : 2022-10-04 Nicolas Bolik-Coulon, D. Flemming Hansen, Lewis E. Kay
-
Characterization of conformational heterogeneity via higher-dimensionality, proton-detected solid-state NMR J. Biomol. NMR (IF 2.7) Pub Date : 2022-09-23 Ekaterina Burakova, Suresh K. Vasa, Rasmus Linser
-
Measurement of 1Hα transverse relaxation rates in proteins: application to solvent PREs J. Biomol. NMR (IF 2.7) Pub Date : 2022-08-26 Yuki Toyama, Atul Kaushik Rangadurai, Lewis E. Kay
-
The measurement of binding affinities by NMR chemical shift perturbation J. Biomol. NMR (IF 2.7) Pub Date : 2022-08-03 Billy Hobbs, Jack Drant, Mike P. Williamson
-
Proton TOCSY NMR relaxation rates quantitate protein side chain mobility in the Pin1 WW domain J. Biomol. NMR (IF 2.7) Pub Date : 2022-07-21 Gaddafi I. Danmaliki, Peter M. Hwang
-
Distinct stereospecific effect of chiral tether between a tag and protein on the rigidity of paramagnetic tag J. Biomol. NMR (IF 2.7) Pub Date : 2022-07-16 Jia-Liang Chen, Bin Li, Bo Ma, Xun-Cheng Su
-
Metabolic15N labeling of the N-glycosylated immunoglobulin G1 Fc with an engineered Saccharomyces cerevisiae strain J. Biomol. NMR (IF 2.7) Pub Date : 2022-07-08 Anjali Shenoy, Alexander R. Davis, Elijah T. Roberts, I. Jonathan Amster, Adam W. Barb
-
The time-zero HSQC method improves the linear free energy relationship of a polypeptide chain through the accurate measurement of residue-specific equilibrium constants J. Biomol. NMR (IF 2.7) Pub Date : 2022-06-14 Seiichiro Hayashi, Daisuke Kohda
-
Towards autonomous analysis of chemical exchange saturation transfer experiments using deep neural networks J. Biomol. NMR (IF 2.7) Pub Date : 2022-05-27 Gogulan Karunanithy, Tairan Yuwen, Lewis E. Kay, D. Flemming Hansen
-
Ligand-induced structural transitions combined with paramagnetic ions facilitate unambiguous NMR assignments of methyl groups in large proteins J. Biomol. NMR (IF 2.7) Pub Date : 2022-04-10 Lars Mühlberg, Tuncay Alarcin, Thorben Maass, Robert Creutznacher, Richard Küchler, Alvaro Mallagaray
-
Fundamental and practical aspects of machine learning for the peak picking of biomolecular NMR spectra J. Biomol. NMR (IF 2.7) Pub Date : 2022-04-07 Da-Wei Li, Alexandar L. Hansen, Lei Bruschweiler-Li, Chunhua Yuan, Rafael Brüschweiler
-
77Se-13C based dipolar correlation experiments to map selenium sites in microcrystalline proteins J. Biomol. NMR (IF 2.7) Pub Date : 2022-03-23 Caitlin M. Quinn, Shiping Xu, Guangjin Hou, Qingqing Chen, Deepak Sail, R. Andrew Byrd, Sharon Rozovsky
Sulfur-containing sites in proteins are of great importance for both protein structure and function, including enzymatic catalysis, signaling pathways, and recognition of ligands and protein partners. Selenium-77 is an NMR active spin-1/2 nucleus that shares many physiochemical properties with sulfur and can be readily introduced into proteins at sulfur sites without significant perturbations to the
-
-
Optimization and validation of multi-state NMR protein structures using structural correlations J. Biomol. NMR (IF 2.7) Pub Date : 2022-03-19 Dzmitry Ashkinadze, Harindranath Kadavath, Roland Riek, Peter Güntert
Recent advances in the field of protein structure determination using liquid-state NMR enable the elucidation of multi-state protein conformations that can provide insight into correlated and non-correlated protein dynamics at atomic resolution. So far, NMR-derived multi-state structures were typically evaluated by means of visual inspection of structure superpositions, target function values that
-
Site-specific protein methyl deuterium quadrupolar patterns by proton-detected 3D 2H–13C–1H MAS NMR spectroscopy J. Biomol. NMR (IF 2.7) Pub Date : 2022-01-08 Ümit Akbey
Determination of protein structure and dynamics is key to understand the mechanism of protein action. Perdeuterated proteins have been used to obtain high resolution/sensitivty NMR experiments via proton-detection. These methods utilizes 1H, 13C and 15N nuclei for chemical shift dispersion or relaxation probes, despite the existing abundant deuterons. However, a high-sensitivity NMR method to utilize
-
Monitoring protein unfolding transitions by NMR-spectroscopy J. Biomol. NMR (IF 2.7) Pub Date : 2022-01-04 Matthias Dreydoppel, Jochen Balbach, Ulrich Weininger
NMR-spectroscopy has certain unique advantages for recording unfolding transitions of proteins compared e.g. to optical methods. It enables per-residue monitoring and separate detection of the folded and unfolded state as well as possible equilibrium intermediates. This allows a detailed view on the state and cooperativity of folding of the protein of interest and the correct interpretation of subsequent
-
Glutamine-free mammalian expression of recombinant glycoproteins with uniform isotope labeling: an application for NMR analysis of pharmaceutically relevant Fc glycoforms of human immunoglobulin G1 J. Biomol. NMR (IF 2.7) Pub Date : 2022-01-03 Saeko Yanaka, Hirokazu Yagi, Rina Yogo, Masayoshi Onitsuka, Koichi Kato
Mammalian cells are widely used for producing recombinant glycoproteins of pharmaceutical interest. However, a major drawback of using mammalian cells is the high production costs associated with uniformly isotope-labeled glycoproteins due to the large quantity of labeled l-glutamine required for their growth. To address this problem, we developed a cost-saving method for uniform isotope labeling by
-
Protein resonance assignment by solid-state NMR based on 1H-detected 13C double-quantum spectroscopy at fast MAS J. Biomol. NMR (IF 2.7) Pub Date : 2021-11-23 Alons Lends, Mélanie Berbon, Birgit Habenstein, Yusuke Nishiyama, Antoine Loquet
Solid-state NMR spectroscopy is a powerful technique to study insoluble and non-crystalline proteins and protein complexes at atomic resolution. The development of proton (1H) detection at fast magic-angle spinning (MAS) has considerably increased the analytical capabilities of the technique, enabling the acquisition of 1H-detected fingerprint experiments in few hours. Here an approach based on double-quantum
-
Clustered sparsity and Poisson-gap sampling J. Biomol. NMR (IF 2.7) Pub Date : 2021-11-05 Paweł Kasprzak, Mateusz Urbańczyk, Krzysztof Kazimierczuk
Non-uniform sampling (NUS) is a popular way of reducing the amount of time taken by multidimensional NMR experiments. Among the various non-uniform sampling schemes that exist, the Poisson-gap (PG) schedules are particularly popular, especially when combined with compressed-sensing (CS) reconstruction of missing data points. However, the use of PG is based mainly on practical experience and has not
-
Efficient solvent suppression with adiabatic inversion for 1H-detected solid-state NMR J. Biomol. NMR (IF 2.7) Pub Date : 2021-10-21 Matsunaga, Tatsuya, Okabe, Ryotaro, Ishii, Yoshitaka
This study introduces a conceptually new solvent suppression scheme with adiabatic inversion pulses for 1H-detected multidimensional solid-state NMR (SSNMR) of biomolecules and other systems, which is termed “Solvent suppression of Liquid signal with Adiabatic Pulse” (SLAP). 1H-detected 2D 13C/1H SSNMR data of uniformly 13C- and 15N-labeled GB1 sample using ultra-fast magic angle spinning at a spinning
-
Correction to: An automated iterative approach for protein structure refinement using pseudocontact shifts. J. Biomol. NMR (IF 2.7) Pub Date : 2021-12-01 Stefano Cucuzza,Peter Güntert,Andreas Plückthun,Oliver Zerbe
-
A simple and sensitive detection of the binding ligands by using the receptor aggregation and NMR spectroscopy: a test case of the maltose binding protein J. Biomol. NMR (IF 2.7) Pub Date : 2021-09-15 Chae, Young Kee, Um, Yoonjin, Kim, Hakbeom
Protein-ligand interaction is one of the highlights of molecular recognition. The most popular application of this type of interaction is drug development which requires a high throughput screening of a ligand that binds to the target protein. Our goal was to find a binding ligand with a simple detection, and once this type of ligand was found, other methods could then be used to measure the detailed
-
CSI-LSTM: a web server to predict protein secondary structure using bidirectional long short term memory and NMR chemical shifts J. Biomol. NMR (IF 2.7) Pub Date : 2021-09-12 Miao, Zhiwei, Wang, Qianqian, Xiao, Xiongjie, Kamal, Ghulam Mustafa, Song, Linhong, Zhang, Xu, Li, Conggang, Zhou, Xin, Jiang, Bin, Liu, Maili
Protein secondary structure provides rich structural information, hence the description and understanding of protein structure relies heavily on it. Identification or prediction of secondary structures therefore plays an important role in protein research. In protein NMR studies, it is more convenient to predict secondary structures from chemical shifts as compared to the traditional determination
-
1H R1ρ relaxation dispersion experiments in aromatic side chains J. Biomol. NMR (IF 2.7) Pub Date : 2021-09-12 Dreydoppel, Matthias, Lichtenecker, Roman J., Akke, Mikael, Weininger, Ulrich
Aromatic side chains are attractive probes of protein dynamic, since they are often key residues in enzyme active sites and protein binding sites. Dynamic processes on microsecond to millisecond timescales can be studied by relaxation dispersion experiments that attenuate conformational exchange contributions to the transverse relaxation rate by varying the refocusing frequency of applied radio-frequency
-
Evaluation of the tert-butyl group as a probe for NMR studies of macromolecular complexes J. Biomol. NMR (IF 2.7) Pub Date : 2021-09-09 Voleti, Rashmi, Bali, Sofia, Guerrero, Jaime, Smothers, Jared, Springhower, Charis, Acosta, Gerardo A., Brewer, Kyle D., Albericio, Fernando, Rizo, Josep
The development of methyl transverse relaxation optimized spectroscopy has greatly facilitated the study of macromolecular assemblies by solution NMR spectroscopy. However, limited sample solubility and stability has hindered application of this technique to ongoing studies of complexes formed on membranes by the neuronal SNAREs that mediate neurotransmitter release and synaptotagmin-1, the Ca2+ sensor