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NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
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
Structure from chemical shifts:
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:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
Quality Control Check
NMR spectrum prediction:
FANDAS
MestReS
V-NMR
Flexibility from structure:
Backbone S2
Methyl S2
B-factor
Molecular dynamics:
Gromacs
Amber
Antechamber
Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
Camshift
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
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Old 11-20-2010, 06:01 PM
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Default Expression, Purification, Detergent Screening and Solution NMR Backbone Assignment of

Expression, Purification, Detergent Screening and Solution NMR Backbone Assignment of the Human Potassium Channel Accessory Subunit MiRP1.

Expression, Purification, Detergent Screening and Solution NMR Backbone Assignment of the Human Potassium Channel Accessory Subunit MiRP1.

Protein Expr Purif. 2010 Nov 15;

Authors: Chen L, Lai C, Lai J, Tian C

MiRP1 (MinK related protein 1) is a membrane protein in the KCNE family. It can associate with and modulate various voltage gated potassium channels. Mutations in human MiRP1 have been found to cause many congenital and acquired long QT syndromes, which are potentially life-threatening cardiac arrhythmias. Here, human MiRP1 was over-expressed in E. coli, purified and eluted into different detergents. Two dimensional (1)H-(15)N correlated solution nuclear magnetic resonance (NMR) spectra of the human MiRP1 in four different detergent micelles indicated that high resolution solution NMR spectrum can be obtained for human MiRP1 in detergent lyso-myristoylphosphatidylglycerol (LMPG). Circular dichroism (CD) spectroscopy of human MiRP1 indicated a high content of alpha-helical secondary structure in LMPG. Backbone assignments of most MiRP1 residues were achieved through a series of triple resonance NMR experiments. Secondary structure analysis based on backbone chemical shifts showed several stretches of alpha-helices along the primary sequence of MiRP1 in LMPG.

PMID: 21087668 [PubMed - as supplied by publisher]



Source: PubMed
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