Welcome to The Cavagnero Group!
The Cavagnero Group is a research group at the University of Wisconsin-Madison that is interested in protein folding, especially in environments similar to those found in real life inside cells.
See our old website at: http://www.chem.wisc.edu/~cavagnero/index.htm
The mechanism of protein folding is one of the most fundamental unanswered questions in modern chemistry and biology. Most prior folding studies have focused on the in vitro folding of fully formed (i.e., full-length) biopolymers starting from non-physiologically relevant unfolded states generated by high concentrations of denaturants, temperature-jumps. But how do proteins "really" fold inside a cell? The goal of our research is to gain a structural and dynamic understanding of the cotranslational and immediately post-translational folding pathways of soluble single-domain proteins in the cell. We work both in the presence and absence of molecular chaperones, under physiologically relevant conditions. This research direction differentiates our group’s efforts from most prior work on both in vivo and in vitro folding.
The specific aims of our group are to:
- follow the conformational changes relevant to understanding the folding of polypeptides and proteins as they emerge from the ribosome,
- compare and contrast in vitro and in vivo folding mechanisms, and
- establish closer links between protein folding theory and experiments.
Some of the main tools/techniques used in our lab are:
|Spectroscopic/Computational Techniques||Biochemical Techniques|
Our work so far has mainly focused on single-domain, predominantly a-helical proteins.