Translocation of biopolymers through biological or solid state nanopores has attracted a great deal of attention from experimentalists, theoreticians, and engineers.

 Information Theory

Protein Aggregation and Amyloid

Protein Folding

Hidden Markov Models

The Talaga Lab in active in two types of single molecule spectroscopy.

Michael Vitarelli successfully defended his dissertation today. Congratulations Dr. Vitarelli

16 Oct

The Talaga lab is focussed on studying the molecular-level basis for structural changes in proteins. We use a variety of biophysical techniques ranging from dynamic light scattering to atomic force microscopy to single molecule fluorescence. We are actively developing new methods in the area of single molecule fluorescence spectroscopy to increase our ability to understand the role of structural changes and fluctuations as they occur at "equilibrium" by allowing us to observe them in real time. A typical project in the Talaga group will include producing the protein of interest by expressing it in E. coli, characterizing the protein with traditional bulk measurements, and performing advanced single molecule measurements on the protein while it is engaged in the dynamic activity we are seeking to characterize. Some of the dynamic structure-function relationships we are investigating include:   

  • protein/peptide secondary structure fluctuations at the 1 or 2 amino acid level;
  • protein folding and unfolding with particular emphasis on visualizing the transition state;
  • protein misfolding and assembly into ß-amyloid fibrils;
  • protein hydrophobic core fluctuations and their connection to protein stability;
  • protein structural fluctuations and their role in substrate/ligand recognition.

Please click through to our Research Pages for more details about our ongoing scientific activities.

Citation Report from Web of Science generated August 2013.


Aleksey Vishnyakov, David S. Talaga, and Alexander V. Neimark, DPD Simulation of Protein Conformations: From α‐Helices to β‐Structures. J Phys Chem Lett 2012, 3, 3081-3087.