[NMR paper] Monothiol and dithiol glutaredoxin-1 from Clostridium oremlandii: identification of domain-swapped structures by NMR, X-ray crystallography and HDX mass spectrometry.
Monothiol and dithiol glutaredoxin-1 from Clostridium oremlandii: identification of domain-swapped structures by NMR, X-ray crystallography and HDX mass spectrometry.
Related ArticlesMonothiol and dithiol glutaredoxin-1 from Clostridium oremlandii: identification of domain-swapped structures by NMR, X-ray crystallography and HDX mass spectrometry.
IUCrJ. 2020 Nov 01;7(Pt 6):1019-1027
Authors: Lee K, Yeo KJ, Choi SH, Lee EH, Kim BK, Kim S, Cheong HK, Lee WK, Kim HY, Hwang E, Woo JR, Lee SJ, Hwang KY
Abstract
Protein dimerization or oligomerization resulting from swapping part of the protein between neighboring polypeptide chains is known to play a key role in the regulation of protein function and in the formation of protein aggregates. Glutaredoxin-1 from Clostridium oremlandii (cGrx1) was used as a model to explore the formation of multiple domain-swapped conformations, which were made possible by modulating several hinge-loop residues that can form a pivot for domain swapping. Specifically, two alternative domain-swapped structures were generated and analyzed using nuclear magnetic resonance (NMR), X-ray crystallography, circular-dichroism spectroscopy and hydrogen/deuterium-exchange (HDX) mass spectrometry. The first domain-swapped structure (?3-swap) was formed by the hexameric cGrx1-cMsrA complex. The second domain-swapped structure (?1-swap) was formed by monothiol cGrx1 (C16S) alone. In summary, the first domain-swapped structure of an oxidoreductase in a hetero-oligomeric complex is presented. In particular, a single point mutation of a key cysteine residue to serine led to the formation of an intramolecular disulfide bond, as opposed to an intermolecular disulfide bond, and resulted in modulation of the underlying free-energy landscape of protein oligomerization.
[NMR paper] Accurate Identification of Unknown and Known Metabolic Mixture Components by Combining 3D NMR with Fourier Transform Ion Cyclotron Resonance Tandem Mass Spectrometry.
Accurate Identification of Unknown and Known Metabolic Mixture Components by Combining 3D NMR with Fourier Transform Ion Cyclotron Resonance Tandem Mass Spectrometry.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Accurate Identification of Unknown and Known Metabolic Mixture Components by Combining 3D NMR with Fourier Transform Ion Cyclotron Resonance Tandem Mass Spectrometry.
J Proteome Res. 2017 Oct 06;16(10):3774-3786
Authors: Wang C, He L, Li DW, Bruschweiler-Li L,...
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[NMR paper] An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of ?1 -antitrypsin upon ligand binding.
An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of ?1 -antitrypsin upon ligand binding.
An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of ?1 -antitrypsin upon ligand binding.
Protein Sci. 2015 May 26;
Authors: Nyon MP, Prentice T, Day J, Kirkpatrick J, Sivalingam GN, Levy G, Haq I, Irving JA, Lomas DA, Christodoulou J, Gooptu B, Thalassinos K
...
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05-27-2015 10:39 AM
An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of ?1-antitrypsin upon ligand binding
An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of ?1-antitrypsin upon ligand binding
Abstract
Native mass spectrometry (MS) methods permit the study of multiple protein species within solution equilibria, whilst ion mobility (IM)-MS can report on conformational behaviour of specific states. We used IM-MS to study a conformationally labile protein (?1-antitrypsin) that undergoes pathological polymerisation in the context of point mutations. The folded, native state of the Z variant remains...
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05-26-2015 08:09 PM
Massive mass spectrometry for viruses
Massive mass spectrometry for viruses
http://www.spectroscopynow.com/common/images/thumbnails/145236699a2.jpgScientists in the US have examined the massive protein shells that hold virus DNA, known as procapsids, using charge detection mass spectrometry to identify entities more than 23 megaDaltons in size.
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04-02-2014 11:54 PM
[NMR paper] Identification of differential protein binding affinities in an atropisomeric pharmaceutical compound using non-covalent mass spectrometry, equilibrium dialysis and NMR.
Identification of differential protein binding affinities in an atropisomeric pharmaceutical compound using non-covalent mass spectrometry, equilibrium dialysis and NMR.
Related Articles Identification of differential protein binding affinities in an atropisomeric pharmaceutical compound using non-covalent mass spectrometry, equilibrium dialysis and NMR.
Anal Chem. 2013 May 22;
Authors: Maple HJ, Garlish RA, Whitcombe I, Hold A, Prosser CE, Ford D, Mackenzie H, Crosby J, Porter J, Taylor RJ, Crump MP
Abstract
Atropisomerism of...
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05-24-2013 10:44 PM
[NMR paper] X-ray crystallography and NMR studies of domain-swapped canecystatin-1.
X-ray crystallography and NMR studies of domain-swapped canecystatin-1.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles X-ray crystallography and NMR studies of domain-swapped canecystatin-1.
FEBS J. 2013 Feb;280(4):1028-38
Authors: Valadares NF, de Oliveira-Silva R, Cavini IA, Marques Ide A, Pereira HD, Soares-Costa A, Henrique-Silva F, Kalbitzer HR, Munte CE, Garratt RC
Abstract
The three-dimensional structure of...
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04-12-2013 10:34 AM
[NMR paper] The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliat
The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures.
Related Articles The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures.
Structure. 2002 May;10(5):673-86
Authors: Barrientos LG, Louis JM, Botos I, Mori T, Han Z, O'Keefe BR, Boyd MR, Wlodawer A, Gronenborn AM
The structure of the potent HIV-inactivating protein cyanovirin-N was previously found by NMR to be a monomer in solution and a domain-swapped dimer by X-ray...
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11-24-2010 08:49 PM
[NMR paper] Mass spectrometry--a useful tool for the protein X-ray crystallographer and NMR spect
Mass spectrometry--a useful tool for the protein X-ray crystallographer and NMR spectroscopist.
Related Articles Mass spectrometry--a useful tool for the protein X-ray crystallographer and NMR spectroscopist.
Structure. 1994 Jun 15;2(6):465-7
Authors: Chait BT
Monothiol and dithiol glutaredoxin-1 from Clostridium oremlandii: identification of domain-swapped structures by NMR, X-ray crystallography and HDX mass spectrometry.
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