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Mol Cell Proteomics. 2011 Oct;10(10):M110.006841. doi: 10.1074/mcp.M110.006841. Epub 2011 Jun 22.

Cross-linking measurements of in vivo protein complex topologies.

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Department of Chemistry, Washington State University, Pullman, WA 99164, USA.


Identification and measurement of in vivo protein interactions pose critical challenges in the goal to understand biological systems. The measurement of structures and topologies of proteins and protein complexes as they exist in cells is particularly challenging, yet critically important to improve understanding of biological function because proteins exert their intended function only through the structures and interactions they exhibit in vivo. In the present study, protein interactions in E. coli cells were identified in our unbiased cross-linking approach, yielding the first in vivo topological data on many interactions and the largest set of identified in vivo cross-linked peptides produced to date. These data show excellent agreement with protein and complex crystal structures where available. Furthermore, our unbiased data provide novel in vivo topological information that can impact understanding of biological function, even for cases where high resolution structures are not yet available.

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