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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
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
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Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
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TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
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Chemical shifts re-referencing:
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UNIO Shiftinspector
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Vasco
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Protein geomtery:
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What-If
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PSVS
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SAVES2 or SAVES4
Vadar
Prosa
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V-NMR
Flexibility from structure:
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Methyl S2
B-factor
Molecular dynamics:
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From structure:
Shiftx2
Sparta+
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CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
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From sequence:
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Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
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Default NMR resonance assignment and backbone dynamics of a C-terminal domain homolog of orange carotenoid protein.

NMR resonance assignment and backbone dynamics of a C-terminal domain homolog of orange carotenoid protein.

Related Articles NMR resonance assignment and backbone dynamics of a C-terminal domain homolog of orange carotenoid protein.

Biomol NMR Assign. 2020 Sep 16;:

Authors: Maksimov EG, Laptev GY, Blokhin DS, Klochkov VV, Slonimskiy YB, Sluchanko NN, Friedrich T, Chang CF, Polshakov VI

Abstract
Photoprotection in cyanobacteria is mediated by the Orange Carotenoid Protein (OCP), a two-domain photoswitch which has multiple natural homologs of its N- and C-terminal domains. Recently, it was demonstrated that C-terminal domain homologs (CTDHs) of OCP are standalone carotenoproteins participating in multidirectional carotenoid transfer between membranes and proteins. Non-covalent embedment of a*ketocarotenoid causes dimerization of the small 16-kDa water-soluble CTDH protein; however, dynamic interactions of CTDH with membranes and other proteins apparently require the monomeric state. Although crystallography recently provided static snapshots of the Anabaena CTDH (AnaCTDH) spatial structure in the apo-form, which predicted mobility of some putative functional segments, no crystallographic information on the holo-form of CTDH is presently available. In order to use NMR techniques to cope with the dynamics of the AnaCTDH protein, it was necessary to obtain 1H, 13C and 15N resonance assignments. AnaCTDH samples enriched with 13C and 15N isotopes were prepared using recombinant protein expression, and NMR resonance assignment was achieved for more than 90% of the residues.*The obtained results revealed that the structure of AnaCTDH in solution and in the*crystal are largely equivalent. Together with 15N NMR relaxation experiments, our data shed light on the AnaCTDH dynamics and provide the platform for the subsequent analysis of the holo-CTDH structure in solution, for the better understanding of light-triggered protein-protein interactions and the development of antioxidant nanocarriers for biomedical applications in the future.


PMID: 32939684 [PubMed - as supplied by publisher]



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