A folding pathway-dependent score to recognize membrane proteins

PLoS One. 2011 Mar 1;6(3):e16778. doi: 10.1371/journal.pone.0016778.

Abstract

While various approaches exist to study protein localization, it is still a challenge to predict where proteins localize. Here, we consider a mechanistic viewpoint for membrane localization. Taking into account the steps for the folding pathway of α-helical membrane proteins and relating biophysical parameters to each of these steps, we create a score capable of predicting the propensity for membrane localization and call it FP(3)mem. This score is driven from the principal component analysis (PCA) of the biophysical parameters related to membrane localization. FP(3)mem allows us to rationalize the colocalization of a number of channel proteins with the Cav1.2 channel by their fewer propensities for membrane localization.

MeSH terms

  • Animals
  • Calcium Channels
  • Databases, Protein
  • Eukaryotic Cells / metabolism
  • Humans
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism*
  • Prokaryotic Cells / metabolism
  • Protein Folding*
  • Protein Structure, Secondary
  • Protein Transport
  • Receptors, AMPA / metabolism
  • Receptors, N-Methyl-D-Aspartate / metabolism

Substances

  • Calcium Channels
  • Membrane Proteins
  • Receptors, AMPA
  • Receptors, N-Methyl-D-Aspartate