Cellular and Molecular Life Sciences

, 66:2231

Functional aspects of protein flexibility

Authors

  • Kaare Teilum
    • Structural Biology and NMR Laboratory (SBiN-Lab), Department of BiologyUniversity of Copenhagen
  • Johan G. Olsen
    • Structural Biology and NMR Laboratory (SBiN-Lab), Department of BiologyUniversity of Copenhagen
    • Structural Biology and NMR Laboratory (SBiN-Lab), Department of BiologyUniversity of Copenhagen
Review

DOI: 10.1007/s00018-009-0014-6

Cite this article as:
Teilum, K., Olsen, J.G. & Kragelund, B.B. Cell. Mol. Life Sci. (2009) 66: 2231. doi:10.1007/s00018-009-0014-6

Abstract

Proteins are dynamic entities, and they possess an inherent flexibility that allows them to function through molecular interactions within the cell, among cells and even between organisms. Appreciation of the non-static nature of proteins is emerging, but to describe and incorporate this into an intuitive perception of protein function is challenging. Flexibility is of overwhelming importance for protein function, and the changes in protein structure during interactions with binding partners can be dramatic. The present review addresses protein flexibility, focusing on protein–ligand interactions. The thermodynamics involved are reviewed, and examples of structure-function studies involving experimentally determined flexibility descriptions are presented. While much remains to be understood about protein flexibility, it is clear that it is encoded within their amino acid sequence and should be viewed as an integral part of their structure.

Keywords

Protein dynamics Protein–ligand interactions Protein flexibility Flexible protein recognition model Entropy Intrinsically disordered proteins

Copyright information

© Birkhäuser Verlag, Basel/Switzerland 2009