Priv. Doz. Dr. Günther WoehlkeKinesins carry cellular cargo along microtubule filaments to their sites of destiny. They couple the chemical energy from ATP hydrolysis to mechanical work. We have studied this process extensively using kinetic and microscopic assays, as well as laser traps and single-molecule fluorescence. Another type of mechanochemical enzymes are spastin and katanin, which use ATP to remove tubulin subunits out of the microtubule lattice. We are currently setting up assays to tackle the coupling of the kinetic cycle and the mechanical effect, microtubule breakage. |
Latest PublicationsAlternating-site mechanism of kinesin-1 characterized by single-molecule FRET using fluorescent ATP analogues
Biophys J. 97:173-82 Link: www.ncbi.nlm.nih.gov/pubmed/19580755
Alternating-site mechanism of kinesin-1 characterized by single-molecule FRET using fluorescent ATP analogues.
Biophys J. ;97(1):173-82. PubMed PMID: 19580755; PubMed Central PMCID: PMC2711353.
Properties of the kinesin-3 NcKin3 motor domain and implications for neck function.
FEBS J. 2009 Jul;276(13):3641-55. PubMed PMID: 19490122
|
Research Area
|
Random Pic
|


