Proteomic studies of the intrinsically unstructured mammalian proteome

J Proteome Res. 2006 Oct;5(10):2839-48. doi: 10.1021/pr060328c.

Abstract

Intrinsically unstructured proteins (IUPs) represent an important class of proteins primarily involved in cellular signaling and regulation. The aim of this study was to develop methodology for the enrichment and identification of IUPs. We show that heat treatment of NIH3T3 mouse fibroblast cell extracts at 98 degrees C selects for IUPs. The majority of these IUPs were cytosolic or nuclear proteins involved in cell signaling or regulation. These studies represent the first large-scale experimental investigation of the intrinsically unstructured mammalian proteome.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Nucleus / chemistry
  • Cytosol / chemistry
  • Electrophoresis, Gel, Two-Dimensional
  • Hot Temperature
  • Hydrophobic and Hydrophilic Interactions
  • Mice
  • NIH 3T3 Cells
  • Nuclear Proteins / analysis
  • Protein Conformation
  • Protein Denaturation
  • Proteins / analysis*
  • Proteome / analysis*
  • Proteomics / methods*
  • Signal Transduction*

Substances

  • Nuclear Proteins
  • Proteins
  • Proteome