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NMR processing:
MDD
NMR assignment:
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MARS
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PINE
Side-chains:
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NOEs:
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UNIO Candid
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Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
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Fragment-based:
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Refinement:
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Fragment-based:
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Homology-based:
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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MICS caps, β-turns
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
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Protein geomtery:
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Methyl S2
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Molecular dynamics:
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From structure:
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CH3shift- Methyl
ArShift- Aromatic
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PPM
CheShift-2- Cα
From sequence:
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Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
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Default 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 Articles Monothiol 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.


PMID: 33209316 [PubMed]



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