Capturing dynamic protein interactions

See allHide authors and affiliations

Science  09 Mar 2018:
Vol. 359, Issue 6380, pp. 1105-1106
DOI: 10.1126/science.aat0576

You are currently viewing the summary.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution


Protein-protein interactions form the molecular basis for organismal development and function (1, 2). In cells, protein interactions are dynamic and subject to spatiotemporal regulations that are specific to the cell type and cell cycle phase. Mutations that abolish or rewire protein-protein interaction networks (the interactome) are often detrimental and manifest in developmental anomalies and diseases (3, 4). Recent advances in quantitative proteomics offer snapshots of cell type–specific proteomes, but scientific understanding of how protein-protein interactions vary between physiological and disease conditions is limited. On page 1170 of this issue, Tan et al. report a technique for inferring dynamics of protein interactions by characterizing protein thermal stability upon heat denaturation (5).