Relaxation, equilibrium oligomerization, and molecular symmetry of the VASP (336-380) EVH2 tetramer.

@article{Zimmermann2002RelaxationEO,
  title={Relaxation, equilibrium oligomerization, and molecular symmetry of the VASP (336-380) EVH2 tetramer.},
  author={J{\"u}rgen Zimmermann and Dirk Labudde and Thomas Jarchau and Ulrich Walter and Hartmut Oschkinat and L. J. Ball},
  journal={Biochemistry},
  year={2002},
  volume={41 37},
  pages={11143-51}
}
An investigation of the structural and dynamic properties of the C-terminal fragment of the human protein VASP (VASP 336-380) has been performed. Full length VASP has been shown to be tetrameric in solution, and the C-terminal 45 residues of the protein have been suggested to be responsible for the oligomerization. We have expressed and purified a C… CONTINUE READING