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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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Unread 08-07-2012, 05:55 PM
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Default Postdoc

Postdoc

Postdoctoral positions are available in the research group of Professor Josh Wand in the Department of Biochemistry & Biophysics and the Johnson Research Foundation of the University of Pennsylvania Perelman School of Medicine. Located in Philadelphia, the University of Pennsylvania is a cosmopolitan center of advanced research across the spectrum of the life and physical sciences. Areas of current interest in the Wand laboratory are creative uses of high pressure NMR to explore protein structural cooperativity; NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids to examine protein hydration and hydration dependent dynamics; uses of reverse micelle encapsulation in structural biology especially membrane-anchored proteins; development and use of advanced NMR relaxation methods to illuminate the character of protein motion and to provide a dynamic proxy for conformational entropy in a variety of functional contexts such as ligand binding, catalysis and evolution; development of NMR data collection strategies and associated software particularly in the realm of sparse sampling; validation of molecular dynamics simulations. Extensive NMR instrumentation is available. See wandlab.org for additional information. Candidates should hold the Ph.D. degree or equivalent and have extensive experience in protein biophysics and/or NMR spectroscopy. Applicants should forward a c.v. and have two letters of reference sent directly to Professor Wand (wand@mail.med.upenn.edu). A. Joshua Wand, Ph.D. Benjamin Rush Professor of Biochemistry & Biophysics Department of Biochemistry & Biophysics University of Pennsylvania Perelman School of Medicine 905 Stellar Chance Laboratories 422 Curie Blvd Philadelphia, PA 19104-6059 telephone 215-573-7288 facsimile 215-573-7290 e-mail wand@mail.med.upenn.edu[IMG]http...s.blogspot.com[/IMG]


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