Capturing dynamic protein interactions: A method based on heat denaturation reveals how proteins interact in different cells

Xiao Han Li (Lead / Corresponding author), Pavithra L. Chavali, M. Madan Babu (Lead / Corresponding author)

Research output: Contribution to journalComment/debatepeer-review

17 Citations (Scopus)

Abstract

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).
Original languageEnglish
Pages (from-to)1105-1106
Number of pages2
JournalScience
Volume359
Issue number6380
DOIs
Publication statusPublished - 9 Mar 2018

ASJC Scopus subject areas

  • General

Fingerprint

Dive into the research topics of 'Capturing dynamic protein interactions: A method based on heat denaturation reveals how proteins interact in different cells'. Together they form a unique fingerprint.

Cite this