Protein Folding
Idea: in this experiment we investigate protein (un)folding
by chemical denaturation of human serum albumin using tryptophan as an intrinsic fluorescent reporter
Biophysics Lab Course, Institute of Biophysics, Ulm University
The folding equilibrium of the plasmaprotein HSA (Human Serum Albumin) is characterized from the fluorescence of a tryptophan residue at position 214.
Successive addition of the denaturant GdmCl leads to an increasing spectral shift of Trp-214 fluorescence, which allows to quantify the increasing fraction of unfolded protein.
The free energy change between folded and unfolded state is determined for two different pH-values by extrapolation to zero denaturant concentration.
Biophysics Lab Course: Gene expression | Bioinformatics | Protein labelling | Protein crystallization | Protein folding | Stopped-flow kinetics | Single-molecule fluorescence | Fluorescence lifetime | Ligand binding | Fluorescence correlation spectroscopy (FCS) | Lipid monolayers | Ion channels | Live cell imaging | Superresolution microscopy | Optical tweezers | AFM
![[Translate to english:] Button Overview Experiments](/fileadmin/website_uni_ulm/nawi.physik/dateien/data/biophyscis_lab/button_overview_experiments_350e.png)
Master of Science in Biophysics
Contact: Prof. Dr. Jens Michaelis, Dr. Carlheinz Röcker, Institute of Biophysics
