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Side-chains:
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UNIO Candid
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Ab initio:
GeNMR
Cyana
XPLOR-NIH
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UNIO ATNOS-Candid
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Fragment-based:
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Template-based:
GeNMR
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Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
CS23D
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
CSI (via RCI server)
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MICS caps, β-turns
d2D
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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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UNIO Shiftinspector
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NMR model quality:
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Flexibility from structure:
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Methyl S2
B-factor
Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
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CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
Shifty
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
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camGroEL
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Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Old 08-04-2020, 12:56 PM
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Default NMR characterization of the C-mannose conformation in a thrombospondin repeat using a selective labeling approach.

NMR characterization of the C-mannose conformation in a thrombospondin repeat using a selective labeling approach.

NMR characterization of the C-mannose conformation in a thrombospondin repeat using a selective labeling approach.

Angew Chem Int Ed Engl. 2020 Aug 03;:

Authors: Jonker HRA, Saxena K, Shcherbakova A, Tiemann B, Bakker H, Schwalbe H

Abstract
Despite the great interest in glycoproteins, structural information reporting on conformation and dynamics of the sugar moieties are limited. We present a new biochemical method to express proteins with glycans that are selectively labeled with NMR active nuclei. We report on the incorporation of 13C-labeled mannose in the C-mannosylated UNC-5 thrombospondin repeat. The conformational landscape of the C-mannose sugar puckers attached to tryptophan residues of UNC-5 is characterized by interconversion between the canonical 1C4 state and the B03 / 1S3 state. This flexibility may be essential for protein folding and stabilization. We foresee that this versatile tool to produce proteins with selective labeled C-mannose can be applied and adjusted to other systems and modifications and potentially paves a way to advance glycoprotein research by unravelling the dynamical and conformational properties of glycan structures and their interactions.


PMID: 32745319 [PubMed - as supplied by publisher]



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