Structures of the reduced and oxidized state of the mutant D24A of yeast thioredoxin 1: insights into the mechanism for the closing of the water cavity
Structures of the reduced and oxidized state of the mutant D24A of yeast thioredoxin 1: insights into the mechanism for the closing of the water cavity
[NMR paper] Is pressure-induced signal loss in NMR spectra for the Leu99Ala cavity mutant of T4 lysozyme due to unfolding?
Is pressure-induced signal loss in NMR spectra for the Leu99Ala cavity mutant of T4 lysozyme due to unfolding?
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full.gif Related Articles Is pressure-induced signal loss in NMR spectra for the Leu99Ala cavity mutant of T4 lysozyme due to unfolding?
Proc Natl Acad Sci U S A. 2015 Mar 3;112(9):E923
Authors: Kitahara R, Mulder FA
PMID: 25630507
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[NMR paper] Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme.
Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme.
Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme.
Biophys J. 2015 Jan 6;108(1):133-145
Authors: Maeno A, Sindhikara D, Hirata F, Otten R, Dahlquist FW, Yokoyama S, Akasaka K, Mulder FA, Kitahara R
Abstract
Although the structure, function, conformational dynamics, and controlled thermodynamics of proteins...
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[NMR paper] Conformational analysis of oxidized peptide fragments of the C-terminal redox center in thioredoxin reductases by NMR spectroscopy.
Conformational analysis of oxidized peptide fragments of the C-terminal redox center in thioredoxin reductases by NMR spectroscopy.
Related Articles Conformational analysis of oxidized peptide fragments of the C-terminal redox center in thioredoxin reductases by NMR spectroscopy.
J Pept Sci. 2014 Mar 6;
Authors: Ruggles EL, Deker PB, Hondal RJ
Abstract
Vicinal disulfide rings (VDRs) occur when a disulfide bond forms between adjacent cysteine residues in a protein and results in a rare eight-membered ring structure. This eight-membered ring...
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[NMR paper] Investigation of the mechanism of action of novel amphipathic peptides: Insights from solid-state NMR studies of oriented lipid bilayers.
Investigation of the mechanism of action of novel amphipathic peptides: Insights from solid-state NMR studies of oriented lipid bilayers.
Related Articles Investigation of the mechanism of action of novel amphipathic peptides: Insights from solid-state NMR studies of oriented lipid bilayers.
Biochim Biophys Acta. 2014 Feb 6;
Authors: Fillion M, Noël M, Lorin A, Voyer N, Auger M
Abstract
We have investigated in the present study the effect of both non-selective and selective cationic 14-mer peptides on the lipid orientation of DMPC bilayers...
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[NMR paper] 13C-, 15N- and 31P-NMR studies of oxidized and reduced low molecular mass thioredoxin
13C-, 15N- and 31P-NMR studies of oxidized and reduced low molecular mass thioredoxin reductase and some mutant proteins.
Related Articles 13C-, 15N- and 31P-NMR studies of oxidized and reduced low molecular mass thioredoxin reductase and some mutant proteins.
Eur J Biochem. 2004 Apr;271(8):1437-52
Authors: Eisenreich W, Kemter K, Bacher A, Mulrooney SB, Williams CH, Müller F
Thioredoxin reductase (TrxR) from Escherichia coli, the mutant proteins E159Y and C138S, and the mutant protein C138S treated with phenylmercuric acetate were...
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[NMR paper] Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by m
Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR.
Related Articles Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR.
Biochemistry. 2000 Oct 17;39(41):12614-22
Authors: Mulder FA, Hon B, Muhandiram DR, Dahlquist FW, Kay LE
The Leu99-->Ala mutant of T4 lysozyme contains a large internal cavity in the core of its C-terminal domain that is capable of reversibly binding small hydrophobic compounds. Although the cavity is completely buried,...
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11-19-2010 08:29 PM
[NMR paper] NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and
NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex.
Related Articles NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex.
Eur J Biochem. 1998 Oct 15;257(2):299-308
Authors: Jeng MF, Reymond MT, Tennant LL, Holmgren A, Dyson HJ
The mechanism of disulfide reduction by thioredoxin in the cell is thought to occur through the formation and subsequent destruction of a mixed-disulfide intermediate between...
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[NMR paper] 1H, 13C, 15N-NMR resonance assignments of oxidized thioredoxin h from the eukaryotic
1H, 13C, 15N-NMR resonance assignments of oxidized thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii using new methods based on two-dimensional triple-resonance NMR spectroscopy and computer-assisted backbone assignment.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H, 13C, 15N-NMR resonance assignments of oxidized thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii using new methods based on two-dimensional triple-resonance...
Structures of the reduced and oxidized state of the mutant D24A of yeast thioredoxin 1: insights into the mechanism for the closing of the water cavity
Linear Mode
