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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 02-18-2011, 12:02 AM
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Default Postdoctoral Fellow in Protein NMR and Biophysics, University of Colorado Anschutz Medical Campus

University of Colorado Anschutz Medical Campus
Postdoctoral Fellow in Protein NMR and Biophysics

The Department of Pharmaceutical Sciences is seeking applicants for a full-time postdoctoral fellow in protein NMR and Biophysics in the laboratory of Dr. Krishna Mallela. This position will be conducting structure-function studies on disease-related muscle proteins (Singh et al., PNAS 107 (2010) 15069 - 15074) using NMR and other biophysical techniques. The successful applicant will also contribute to the preparation of research publications and laboratory administration, and will be given ample time for their career development.

The minimum qualification is a PhD in biophysics, biochemistry, molecular biology, biophysical chemistry, pharmaceutical sciences or a closely related field. Candidates who are motivated to work independently, possess effective communication skills, and are proficient in protein NMR and biophysics are highly desirable. Salary will be commensurate with the applicant’s qualifications. This position is eligible for individual and dependent health care plans that include medical, dental, disability, and life insurance benefits.

Applicants, please apply electronically at www.jobsatcu.com to job posting number 812566. Applicants must submit electronically a letter of interest, curriculum vitae and the names of three references with regular and e-mail addresses, phone and fax numbers. Any questions regarding this position’s responsibilities can be directed to Dr. Krishna Mallela (Krishna.Mallela@ucdenver.edu) or questions regarding the application process can be directed to Jay Rodenburg, Director of Personnel at jay.rodenburg@ucdenver.edu or at 303/724-2648. Review of applications will begin on March 1, 2011 and will continue until the position is filled.

The University of Colorado is committed to diversity and equality in education and employment.
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