Teaching

Physical Methods for Biomedical Scientists (BME 4903, Spring 2014):

The course will introduce the spectrum of biophysical techniques used in biomedical sciences with a focus on advanced fluorescence spectroscopy. The first half of the course (January to Spring break) will introduce the concepts behind techniques such as: dynamic light scattering, SPR, analytical ultracentrifugation size-exclusion and affinity chromatography, atomic force microscopy, fluorescence spectroscopy, FRET, FTIR, circular dichroism, fluorescence correlation spectroscopy, sub-diffraction microscopy. The second half of the course will be held as six 3 h block lab classes (Fridays 10a - 1p) in which the students will use these techniques in experiments on protein folding, protein stability and amyloid formation. Prior attendance of BME 461 "Protein structure and dynamics" is encouraged. Because of limited room in the experimental lab, attendance will be limited to 9 students. Prereqs: senior or graduate standing

 

Protein Structure and Dynamics (BME 461, Fall 2014):

This course covers the concepts and methods involved in the analysis of protein structure, stability, folding and misfolding. Topics include, protein structural elements, amyloid structure, intra- and intermolecular forces, folding pathways and intermediates, phi-value analysis, kinetics of protein folding and of amyloid formation, spectroscopic methods, fluorescence-based methods, hydrodynamic methods, relaxation techniques and force spectroscopy in measuring dynamics of protein structure and protein interaction, introduction to X-ray crystallography and NMR and their application to problems of bioengineering and biophysics. One half of the course will consist of lectures, the other half will be a student seminar, in which each student presents a paper from primary literature and its concept and methodology that is discussed in detail.Prerequisites: senior or graduate level, prior coursework in physical chemistry / thermodynamics.

 

Introduction to Biomedical Engineering (BME 140, Fall 2014):

Dr. Bieschke teaches one lecture in the introductory BME 140 class, covering the basic principles of protein structure, protein stability and protein folding.

 

 

 

 

 

Age-Related Protein Misfolding

Laboratory of Jan Bieschke, Ph.D.

Center for Biological and Systems Engineering

Age-Related Protein Misfolding

Laboratory of Jan Bieschke, Ph.D.

Center for Biological and Systems Engineering

Age-Related Protein Misfolding

Laboratory of Jan Bieschke, Ph.D.

Center for Biological and Systems Engineering