[NMR paper] High Resolution NMR H/D Exchange of Human Superoxide Dismutase Inclusion Bodies Reveals Significant Native Features Despite Structural Heterogeneity
Protein aggregation is central to aging, disease and biotechnology. While there has been recent progress in defining structural features of cellular protein aggregates, many aspects remain unclear due to heterogeneity of aggregates presenting obstacles to characterization. Here we report high-resolution analysis of cellular inclusion bodies (IBs) of immature human superoxide dismutase (SOD1) mutants using NMR quenched amide hydrogen/deuterium exchange (qHDX), FTIR and Congo red binding. The...
[NMR paper] High-resolution three-dimensional NMR structure of the KRAS proto-oncogene promoter reveals key features of a G-quadruplex involved in transcriptional regulation.
High-resolution three-dimensional NMR structure of the KRAS proto-oncogene promoter reveals key features of a G-quadruplex involved in transcriptional regulation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_final.gif Related Articles High-resolution three-dimensional NMR structure of the KRAS proto-oncogene promoter reveals key features of a G-quadruplex involved in transcriptional regulation.
J Biol Chem. 2017 May 12;292(19):8082-8091
Authors: Kerkour A,...
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[NMR paper] Practical applications of hydrostatic pressure to refold proteins from inclusion bodies for NMR structural studies.
Practical applications of hydrostatic pressure to refold proteins from inclusion bodies for NMR structural studies.
Related Articles Practical applications of hydrostatic pressure to refold proteins from inclusion bodies for NMR structural studies.
Protein Eng Des Sel. 2013 Mar 22;
Authors: Ogura K, Kobashigawa Y, Saio T, Kumeta H, Torikai S, Inagaki F
Abstract
Recently, the hydrostatic pressure refolding method was reported as a practical tool for solubilizing and refolding proteins from inclusion bodies; however, there have been...
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[NMR paper] A solution (17)O-NMR approach for observing an oxidized cysteine residue in Cu,Zn-superoxide dismutase.
A solution (17)O-NMR approach for observing an oxidized cysteine residue in Cu,Zn-superoxide dismutase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles A solution (17)O-NMR approach for observing an oxidized cysteine residue in Cu,Zn-superoxide dismutase.
Chem Commun (Camb). 2013 Jan 22;49(14):1449-51
Authors: Hanashima S, Fujiwara N, Matsumoto K, Iwasaki N, Zheng GQ, Torigoe H, Suzuki K, Taniguchi N, Yamaguchi Y
Abstract
Solution (17)O-NMR application to biological...
NMR Characterization of a “Fibril-Ready” State of Demetalated Wild-Type Superoxide Dismutase
NMR Characterization of a “Fibril-Ready” State of Demetalated Wild-Type Superoxide Dismutase
Lucia Banci, Ivano Bertini, Olga Blaževitš, Francesca Cantini, Moreno Lelli, Claudio Luchinat, Jiafei Mao and Miguela Vieru
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1069689/aop/images/medium/ja-2010-069689_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1069689
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http://feeds.feedburner.com/~r/acs/jacsat/~4/uAjKy7vWoHs
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12-17-2010 12:50 AM
[NMR paper] Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected
Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosis.
Related Articles Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosis.
Biochemistry. 2003 Feb 25;42(7):1890-9
Authors: Shipp EL, Cantini F, Bertini I, Valentine JS, Banci L
The backbone assignment of the copper-zinc superoxide dismutase...
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11-24-2010 09:01 PM
Oxidation of Histidine Residues in Copper-Zinc Superoxide Dismutase by Bicarbonate-St
Oxidation of Histidine Residues in Copper-Zinc Superoxide Dismutase by Bicarbonate-Stimulated Peroxidase and Thiol Oxidase Activities: Pulse EPR and NMR Studies
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi1010305/aop/images/medium/bi-2010-010305_0006.gif
Biochemistry
DOI: 10.1021/bi1010305
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11-24-2010 07:12 AM
[NMR paper] Spectroscopic characterization of polyethyleneglycol modified superoxide dismutase: 1
Spectroscopic characterization of polyethyleneglycol modified superoxide dismutase: 1H NMR studies on its Cu2Co2 derivative.
Related Articles Spectroscopic characterization of polyethyleneglycol modified superoxide dismutase: 1H NMR studies on its Cu2Co2 derivative.
J Inorg Biochem. 1990 Jun;39(2):149-59
Authors: Banci L, Bertini I, Caliceti P, MonsĂą Scolaro L, Schiavon O, Veronese FM
Spectroscopic methods have been employed in order to understand the molecular basis of the decrease in enzymatic activity of the antiinflammatory enzyme...