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Relevant bibliographies by topics / X-ray crystallography; Multi-clear NMR

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Academic literature on the topic 'X-ray crystallography; Multi-clear NMR'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "X-ray crystallography; Multi-clear NMR"

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Cai, Kai, and John Markley. "NMR as a Tool to Investigate the Processes of Mitochondrial and Cytosolic Iron-Sulfur Cluster Biosynthesis." Molecules 23, no. 9 (2018): 2213. http://dx.doi.org/10.3390/molecules23092213.

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Iron-sulfur (Fe-S) clusters, the ubiquitous protein cofactors found in all kingdoms of life, perform a myriad of functions including nitrogen fixation, ribosome assembly, DNA repair, mitochondrial respiration, and metabolite catabolism. The biogenesis of Fe-S clusters is a multi-step process that involves the participation of many protein partners. Recent biophysical studies, involving X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, mass spectrometry (MS), and small angle X-ray scattering (SAXS), have greatly improved our understanding of these steps. In this review, afte

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Nöllmann, Marcelo, W. Marshall Stark, and Olwyn Byron. "A global multi-technique approach to study low-resolution solution structures." Journal of Applied Crystallography 38, no. 6 (2005): 874–87. http://dx.doi.org/10.1107/s0021889805026191.

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Finding the conformation of large macromolecular complexes has become an important problem in structural biology, which is not always soluble by high-resolution techniques such as X-ray crystallography and NMR spectroscopy. Solution biophysical properties can provide direct or indirect structural information on these large complexes. A general systematic approach to the construction of a structural model of the macromolecule consistent with all the experimental solution properties is currently lacking. In this paper, such an approach is presented, where generalized rigid-body modelling is comb

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Zhong, Tingshan, Jixing Zhao, and Hao Lei. "Trianionic binucleating bis(trityl)/aryloxide ligands and their lithium, magnesium, and zinc complexes." Canadian Journal of Chemistry 98, no. 8 (2020): 453–59. http://dx.doi.org/10.1139/cjc-2020-0139.

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A series of lithium complexes with trianionic bis(trityl)/aryloxide ligands were prepared by triple deprotonation of phenols with two ortho-diarylmethyl substituents. Transmetalation with one of the lithium complexes via salt metathesis resulted in the synthesis of corresponding Mg and Zn complexes, which showed distinct coordination stoichiometry and structures. The metal complexes were characterized by multi-nuclear NMR, UV–vis, and infrared spectroscopy. Additionally, the redox property of a trilithium compound was investigated by electrochemical methods. X-ray crystallography revealed that

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Smith, Gregory L., Hélène P. A. Mercier, and Gary J. Schrobilgen. "Synthesis of [F3S⋮NXeF][AsF6] and Structural Study by Multi-NMR and Raman Spectroscopy, Electronic Structure Calculations, and X-ray Crystallography." Inorganic Chemistry 46, no. 4 (2007): 1369–78. http://dx.doi.org/10.1021/ic061899+.

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Hynson, Robert M. G., Anthony P. Duff, Nigel Kirby, Stephan Mudie, and Lawrence K. Lee. "Differential ultracentrifugation coupled to small-angle X-ray scattering on macromolecular complexes." Journal of Applied Crystallography 48, no. 3 (2015): 769–75. http://dx.doi.org/10.1107/s1600576715005051.

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Small-angle X-ray scattering (SAXS) can provide accurate structural information and low-resolution shapes of macromolecules in solution. The technique is particularly amenable to large protein assemblies, which produce a strong scattering signal. Hence, SAXS can be a powerful tool to elucidate quaternary structure, especially when used in combination with high-resolution structural techniques such as X-ray crystallography and NMR. Sample requirements for SAXS experiments are stringent and only monodispersed samples can be satisfactorily analysed. Often, it is not possible to obtain a stable mo

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Han, Jeongmin, Iktae Kim, Jae-Hyun Park, et al. "A Coil-to-Helix Transition Serves as a Binding Motif for hSNF5 and BAF155 Interaction." International Journal of Molecular Sciences 21, no. 7 (2020): 2452. http://dx.doi.org/10.3390/ijms21072452.

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Human SNF5 and BAF155 constitute the core subunit of multi-protein SWI/SNF chromatin-remodeling complexes that are required for ATP-dependent nucleosome mobility and transcriptional control. Human SNF5 (hSNF5) utilizes its repeat 1 (RPT1) domain to associate with the SWIRM domain of BAF155. Here, we employed X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and various biophysical methods in order to investigate the detailed binding mechanism between hSNF5 and BAF155. Multi-angle light scattering data clearly indicate that hSNF5171–258 and BAF155SWIRM are both monomeric in

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Vialemaringe, Marianne, Marie Jos�phe Bourgeois, Evelyne Montaudon, Christian Courseille, Bernard Barbe, and Isabelle Pianet. "Isofenchylic alcohol derived from a functionalized pinene oxide: unexpected formation and structural confirmation using multi-dimensional NMR spectroscopy and x-ray crystallography." Magnetic Resonance in Chemistry 38, no. 9 (2000): 785–88. http://dx.doi.org/10.1002/1097-458x(200009)38:9<785::aid-mrc734>3.0.co;2-5.

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Putnam, Christopher D., Michal Hammel, Greg L. Hura, and John A. Tainer. "X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution." Quarterly Reviews of Biophysics 40, no. 3 (2007): 191–285. http://dx.doi.org/10.1017/s0033583507004635.

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AbstractCrystallography supplies unparalleled detail on structural information critical for mechanistic analyses; however, it is restricted to describing low energy conformations of macromolecules within crystal lattices. Small angle X-ray scattering (SAXS) offers complementary information about macromolecular folding, unfolding, aggregation, extended conformations, flexibly linked domains, shape, conformation, and assembly state in solution, albeit at the lower resolution range of about 50 Å to 10 Å resolution, but without the size limitations inherent in NMR and electron microscopy studies.

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Rath, Emma, Anthony Duff, Robert Knott, and W. Church. "Small-angle X-ray scattering of BAMLET protein-oleic acid complexes at pH 12." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C420. http://dx.doi.org/10.1107/s2053273314095795.

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BAMLET and HAMLET represent a new class of compound having unrealised potential for treating a broad spectrum of cancers and some multi-drug resistant bacterial infections (Brinkmann et al. 2013; Marks et al. 2013). These compounds are composed of protein (14 to 84 kDa) and oleic acid (282 Da), the latter being the main active component. Hypothesised molten-globularity makes structural determination by NMR and X-ray crystallography very challenging. We carried out small angle X-ray scattering (SAXS) on BAMLET at pH 12 (Rath et al. 2014), the pH at which the complex can be prepared. SAXS showed

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Duff, Michael R., Jasmina S. Redzic, Lucas P. Ryan, et al. "Structure, dynamics and function of the evolutionarily changing biliverdin reductase B family." Journal of Biochemistry 168, no. 2 (2020): 191–202. http://dx.doi.org/10.1093/jb/mvaa039.

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Abstract Biliverdin reductase B (BLVRB) family members are general flavin reductases critical in maintaining cellular redox with recent findings revealing that BLVRB alone can dictate cellular fate. However, as opposed to most enzymes, the BLVRB family remains enigmatic with an evolutionarily changing active site and unknown structural and functional consequences. Here, we applied a multi-faceted approach that combines X-ray crystallography, NMR and kinetics methods to elucidate the structural and functional basis of the evolutionarily changing BLVRB active site. Using a panel of three BLVRB i

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Dissertations / Theses on the topic "X-ray crystallography; Multi-clear NMR"

1

Connolly, Julie Christine. "Synthesis and studies on transition metal complexes incorporating thioether, selenoether and phosphine ligands." Thesis, University of Southampton, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.284650.

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