Disclosing Allostery Through Protein Contact Networks

Methods Mol Biol. 2021:2253:7-20. doi: 10.1007/978-1-0716-1154-8_2.

Abstract

Proteins are located in the twilight zone between chemistry and biology, where a peculiar kind of complexity starts. Proteins are the smallest 'devices' showing a sensible adaptation to their environment by the production of appropriate behavior when facing a specific stimulus. This fact qualifies (from the 'effector' side) proteins as nanomachines working as catalysts, motors, or switches. However (from the sensor side), the need to single out the 'specific stimulus' out of thermal noise qualifies proteins as information processing devices. Allostery corresponds to the modification of the configuration (in a broad sense) of the protein molecule in response to a specific stimulus in a non-strictly local way, thereby connecting the sensor and effector sides of the nanomachine. This is why the 'disclosing' of allostery phenomenon is at the very heart of protein function; in this chapter, we will demonstrate how a network-based representation of protein structure in terms of nodes (aminoacid residues) and edges (effective contacts between residues) is the natural language for getting rid of allosteric phenomena and, more in general, of protein structure/function relationships.

Keywords: Network descriptors; Protein contact networks; Spectral clustering.

MeSH terms

  • Allosteric Regulation
  • Databases, Protein
  • Models, Molecular
  • Protein Conformation
  • Protein Interaction Maps
  • Proteins / chemistry*
  • Proteins / metabolism*
  • Software

Substances

  • Proteins