Disulfide bond formation is fundamentally important for protein structure and constitutes a key mechanism by which cells regulate the intracellular oxidation state. Peroxiredoxins (PRDXs) eliminate reactive oxygen species such as hydrogen peroxide through a catalytic cycle of Cys oxidation and reduction. Additionally, upon Cys oxidation PRDXs undergo extensive conformational rearrangements that may underlie their presently structurally poorly defined functions as molecular chaperones....
[ASAP] Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR
Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR
Laura Troussicot, Alicia Vallet, Mikael Molin, Bjo?rn M. Burmann, and Paul Schanda
https://pubs.acs.org/cms/10.1021/jacs.3c01200/asset/images/medium/ja3c01200_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.3c01200
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05-05-2023 10:31 AM
Disulfide Bond Pattern of Transforming Growth Factor ?-Induced Protein
Disulfide Bond Pattern of Transforming Growth Factor ?-Induced Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00694/20160922/images/medium/bi-2016-006945_0011.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00694
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09-24-2016 05:20 PM
[NMR paper] (13)C-NMR studies on disulfide bond isomerization in bovine pancreatic trypsin inhibitor (BPTI).
(13)C-NMR studies on disulfide bond isomerization in bovine pancreatic trypsin inhibitor (BPTI).
(13)C-NMR studies on disulfide bond isomerization in bovine pancreatic trypsin inhibitor (BPTI).
J Biomol NMR. 2016 Aug 26;
Authors: Takeda M, Miyanoiri Y, Terauchi T, Kainosho M
Abstract
Conformational isomerization of disulfide bonds is associated with the dynamics and thus the functional aspects of proteins. However, our understanding of the isomerization is limited by experimental difficulties in probing it. We explored the...
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08-28-2016 11:03 AM
13 C-NMR studies on disulfide bond isomerization in bovine pancreatic trypsin inhibitor (BPTI)
13 C-NMR studies on disulfide bond isomerization in bovine pancreatic trypsin inhibitor (BPTI)
Abstract
Conformational isomerization of disulfide bonds is associated with the dynamics and thus the functional aspects of proteins. However, our understanding of the isomerization is limited by experimental difficulties in probing it. We explored the disulfide conformational isomerization of the Cys14â??Cys38 disulfide bond in bovine pancreatic trypsin inhibitor (BPTI), by performing an NMR line-shape analysis of its Cys carbon peaks. In this approach, 1D...
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Solid-State NMR Study of the Charge-Transfer Complex between Ubiquinone-8 and Disulfide Bond Generating Membrane Protein DsbB
Solid-State NMR Study of the Charge-Transfer Complex between Ubiquinone-8 and Disulfide Bond Generating Membrane Protein DsbB
Ming Tang, Lindsay J. Sperling, Deborah A. Berthold, Anna E. Nesbitt, Robert B. Gennis and Chad M. Rienstra
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107775w/aop/images/medium/ja-2010-07775w_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107775w
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03-05-2011 02:44 AM
[NMR paper] The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studie
The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.
Related Articles The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.
Protein Sci. 2002 Sep;11(9):2218-29
Authors: Katou H, Kanno T, Hoshino M, Hagihara Y, Tanaka H, Kawai T, Hasegawa K, Naiki H, Goto Y
beta(2)-Microglobulin (beta2-m) is a major component of dialysis-related amyloid fibrils. Although recombinant beta2-m forms needle-like fibrils by in vitro extension reaction at pH...
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11-24-2010 08:58 PM
[NMR paper] 13C NMR chemical shifts can predict disulfide bond formation.
13C NMR chemical shifts can predict disulfide bond formation.
Related Articles 13C NMR chemical shifts can predict disulfide bond formation.
J Biomol NMR. 2000 Oct;18(2):165-71
Authors: Sharma D, Rajarathnam K
The presence of disulfide bonds can be detected unambiguously only by X-ray crystallography, and otherwise must be inferred by chemical methods. In this study we demonstrate that 13C NMR chemical shifts are diagnostic of disulfide bond formation, and can discriminate between cysteine in the reduced (free) and oxidized (disulfide bonded)...
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11-19-2010 08:29 PM
[NMR paper] Engineering out motion: a surface disulfide bond alters the mobility of tryptophan 22
Engineering out motion: a surface disulfide bond alters the mobility of tryptophan 22 in cytochrome b5 as probed by time-resolved fluorescence and 1H NMR experiments.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Engineering out motion: a surface disulfide bond alters the mobility of tryptophan 22 in cytochrome b5 as probed by time-resolved fluorescence and 1H NMR experiments.
Biochemistry. 1999 Apr 20;38(16):5065-75
Authors: Storch EM, Grinstead JS, Campbell AP, Daggett V, Atkins WM
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Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR
Linear Mode
