Saturday, 14 March 2015 08:00

Postdoctoral Research Associate

The Talaga Lab at Montclair State University is recruiting for an postdoctoral research associate position.

The Talaga Lab is investigating the phenomenon of amyloid formation. We have received funding from the NIH to investigate how aggregation of ɑ-synuclein into amyloid like fibrils is influenced by and initiated at interfaces. Water-lipids and water-air interfaces are of particular interest. 
 
 
The research project has the following near-term goals:
  • Elucidate the interfacial contribution to the mechanism of ɑ-synuclein aggregation:
    • What is the relationship between the nature of the interface and the conformational changes that occur in α-synuclein at those interfaces?
    • Which conformational changes lead to aggregation?
    • What are the aggregation reaction intermediates?
  • Create a high-sensitivity reporter reagent to detect conformational changes that lead to amyloid-like aggregation.
    • When do conformational changes occur during the aggregation reaction? 
    • What cellular components can induce this conformational change?
 
The successful candidate will lead a research team of 4-6 Senior undergraduates and MS students. This is an excellent opportunity to develop the skills needed to run a research group at a non-top-10 university.
 
Salary
 
Dependent on experience based on NIH-NRSA Scale. 
 
Qualifications
 
The postdoctoral research associate will investigate the phenomenon of amyloid formation from ɑ-synuclein using a variety of biophysical methods, including, but not limited to:
  • Single Molecule Fluorescence and FRET
  • Thin Film Circular Dichroism
  • Protein Mutagenesis
  • Protein Expression, Isolation, and Purification
  • Protein-Dye Conjugation
  • Atomic Force Microscopy
  • Time-Correlated Single Photon Counting
  • Dynamic & Static Light Scattering
  • Fluorescence Lifetime Analysis
A Ph.D. in Chemistry, Biochemistry, Biophysics, or related field is required. 
 
To apply:
 
Send E-mail to This email address is being protected from spambots. You need JavaScript enabled to view it. with “Postdoc Position 2015: [Your Name]” as the subject line.
Include the following information in the body of your e-mail and *not* as an attachment. Do not include any other materials.
 
  • One paragraph (~500 characters) describing how you became interested in this area of research.
  • One paragraph (~500 characters) commenting on any research in this area that you find particularly notable. 
  • One page (~2500 characters) describing what you would do during the first year in the Talaga Lab in order to achieve the above goals. 
  • URL that links to your online professional presence with your qualifications for the position. (e.g. Linked-In, Personal web page(s), etc.)
 
Please forward this announcement to any outstanding candidates you may know. 
 
Montclair State University is an equal opportunity/affirmative action employer with a strong commitment to diversity.
 
Thursday, 21 September 2000 08:00

Talaga 2000

Talaga, D.; Lau, W.; Roder, H.; Tang, J.; Jia, Y.; DeGrado, W.; Hochstrasser, R. Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy. P Natl Acad Sci Usa 2000, 97, 13021–13026.

Monday, 15 September 2003 08:00

Larry Johnson

NIH:NRSA MARC Senior Fellow. 2003-2004. Design of single molecule cryogenic microscope. 

 

Sunday, 23 December 2007 12:17

Talaga 2007

Talaga, D. S. COCIS: Markov processes in single molecule fluorescence. Curr Opin Colloid Interface Sci 12, 285–296 (2007).

Tuesday, 18 July 2006 04:00

Talaga 2006

Talaga, D. S. Information theoretical approach to single-molecule experimental design and interpretation. J Phys Chem A 2006, 110, 9743–9757.

Saturday, 29 July 2006 08:00

Messina 2006

Messina, T. C.; Kim, H.; Giurleo, J. T.; Talaga, D. S. Hidden Markov model analysis of multichromophore photobleaching. J Phys Chem B 2006, 110, 16366–16376.

Friday, 20 June 2008 04:00

Giurleo 2008 JMB

Giurleo, J. T., He, X. & Talaga, D. S. Beta-lactoglobulin assembles into amyloid through sequential aggregated intermediates. J. Mol. Biol. 381, 1332–1348 (2008).