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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
XPLOR-NIH
ASDP
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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:
Preditor
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Secondary structure from chemical shifts:
CSI (via RCI server)
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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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NMR model quality:
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Pseudocontact shifts:
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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
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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:
sedNMR


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Default DNP MAS NMR on channelrhodopsin-2 [Biophysics and Computational Biology]

DNP MAS NMR on channelrhodopsin-2 [Biophysics and Computational Biology]

Becker-Baldus, J., Bamann, C., Saxena, K., Gustmann, H., Brown, L. J., Brown, R. C. D., Reiter, C., Bamberg, E., Wachtveitl, J., Schwalbe, H., Glaubitz, C....
Date: 2015-08-11

Channelrhodopsin-2 from Chlamydomonas reinhardtii is a light-gated ion channel. Over recent years, this ion channel has attracted considerable interest because of its unparalleled role in optogenetic applications. However, despite considerable efforts, an understanding of how molecular events during the photocycle, including the retinal trans-cis isomerization and the deprotonation/reprotonation of the... Read More


PNAS:
Number: 32
Volume: 112
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