Publications

The Structural and Functional Basis of the p97/Valosin-containing Protein (VCP)-interacting Motif (VIM) Mutually Exclusive Binding of Cofactors to the N-Terminal Domain of P97

Hanzelmann, P. and Schindelin, H., 286(44), 38679-38690, Journal of Biological Chemistry, 2011

This study uses BLI and other techniques to study the interaction between p97/VCP and the VCP-interacting motif (VIM), a domain found in several cofactors for p97/VCP. The Octet RED platform with Streptavidin biosensors was used. Biotinylated VIM peptides were loaded onto biosensors to determine kinetic rate constants for the interaction. BLI also was used for detailed mutational analysis of the VIM motif.

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