[NMR paper] Probing pattern and dynamics of disulfide bridges using synthesis and NMR of an ion channel blocker peptide toxin with multiple diselenide bonds.
Probing pattern and dynamics of disulfide bridges using synthesis and NMR of an ion channel blocker peptide toxin with multiple diselenide bonds.
Related Articles Probing pattern and dynamics of disulfide bridges using synthesis and NMR of an ion channel blocker peptide toxin with multiple diselenide bonds.
Chem Sci. 2016 Apr 21;7(4):2666-2673
Authors: Fehér K, Timári I, Rákosi K, Szolomájer J, Illyés TZ, Bartok A, Varga Z, Panyi G, Tóth GK, Kövér KE
Abstract
Anuroctoxin (AnTx), a 35-amino-acid scorpion toxin containing four...
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis
Abstract The phosphorylation-specific peptidyl-prolyl isomerase Pin1 catalyzes the isomerization of the peptide bond preceding a proline residue between cis and trans isomers. To best understand the mechanisms of Pin1 regulation, rigorous enzymatic assays of isomerization are required. However, most measures of isomerase activity require significant constraints on substrate sequence and only yield rate constants for the cis isomer,
kcatcis and apparent Michaelis constants,
...
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Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
J Biomol NMR. 2011 Sep;51(1-2):21-34
Authors: Greenwood AI, Rogals MJ, De S, Lu KP, Kovrigin EL, Nicholson LK
Abstract
The phosphorylation-specific peptidyl-prolyl isomerase Pin1 catalyzes the isomerization of the peptide bond preceding a proline residue between cis and trans isomers. To best understand the mechanisms of Pin1 regulation,...
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09-30-2011 06:00 AM
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
J Biomol NMR. 2011 Sep;51(1-2):21-34
Authors: Greenwood AI, Rogals MJ, De S, Lu KP, Kovrigin EL, Nicholson LK
Abstract
The phosphorylation-specific peptidyl-prolyl isomerase Pin1 catalyzes the isomerization of the peptide bond preceding a proline residue between cis and trans isomers. To best understand the mechanisms of Pin1 regulation,...
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09-30-2011 05:59 AM
[NMR paper] Thiol/disulfide formation associated with the redox activity of the [Fe3S4] cluster o
Thiol/disulfide formation associated with the redox activity of the cluster of Desulfovibrio gigas ferredoxin II. 1H NMR and Mössbauer spectroscopic study.
Related Articles Thiol/disulfide formation associated with the redox activity of the cluster of Desulfovibrio gigas ferredoxin II. 1H NMR and Mössbauer spectroscopic study.
J Biol Chem. 1994 Mar 18;269(11):8052-8
Authors: Macedo AL, Moura I, Surerus KK, Papaefthymiou V, Liu MY, LeGall J, MĂĽnck E, Moura JJ
Desulfovibrio gigas ferredoxin II (FdII) is a small protein (alpha 4 subunit...
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08-22-2010 03:33 AM
[NMR paper] Disulfide bonds in homo- and heterodimers of EF-hand subdomains of calbindin D9k: sta
Disulfide bonds in homo- and heterodimers of EF-hand subdomains of calbindin D9k: stability, calcium binding, and NMR studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Disulfide bonds in homo- and heterodimers of EF-hand subdomains of calbindin D9k: stability, calcium binding, and NMR studies.
Protein Sci. 1993 Jun;2(6):985-1000
...
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[NMR paper] Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin
Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues.
Related Articles Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues.
J Biomol NMR. 1991 May;1(1):49-64
Authors: Uchida K, Miyake Y, Kainosho M
Four enhanced carbonyl carbon resonances were observed when Streptomyces subtilisin inhibitor (SSI) was labeled by...