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NMR processing:
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Side-chains:
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NOEs:
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UNIO Candid
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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
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Fragment-based:
BMRB CS-Rosetta
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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:
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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
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
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CheckShift
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NMR model quality:
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Pseudocontact shifts:
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Protein geomtery:
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PSVS
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SAVES2 or SAVES4
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NMR spectrum prediction:
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Flexibility from structure:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
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CH3shift- Methyl
ArShift- Aromatic
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PPM
CheShift-2- Cα
From sequence:
Shifty
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
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Isotope labeling:
UPLABEL
Solid-state NMR:
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Old 08-31-2017, 12:14 AM
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Default Selenium and Selenocysteine in Protein Chemistry

Selenium and Selenocysteine in Protein Chemistry


Selenocysteine, the selenium-containing analog of cysteine, is the twenty-first proteinogenic amino acid. Since its discovery almost fifty years ago, it has been exploited in unnatural systems more often than in natural systems. Selenocysteine chemistry has attracted the attention of many chemists in the field of chemical biology due to its high reactivity and resulting utility in various applications including chemical modification, chemical protein (semi-)synthesis, and protein folding, to name a few. In this review, we will focus on the chemistry of selenium and selenocysteine and their utility in protein chemistry.

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