Intrinsically Disordered Proteins: Is Your Protein Disordered?
Intrinsically disordered proteins are proteins (or regions of proteins) which, as a monomer, lack stable tertiary structure under physiological conditions in vitro [Dyson (2011) Q. Rev. Biophys. 44:467]. These fascinating proteins frequently regulate cellular processes, and consequently play a prevalent role in a variety of human diseases, including amyloid diseases, viral infections, cancer, and heart disease [Uversky (2012) Expert Opin. Drug. Discov. 7:475]. Since biophysical techniques often define and manipulate the molecular mechanisms underlying cell regulation and disease, many biophysicists work with proteins that are either disordered or have disordered regions. Examining your favorite protein in light of the disordered protein field could suggest potential molecular mechanisms unique to this protein class, identify useful experimental approaches designed for disordered proteins, and provide clues to more easily handle your protein [Mitrea et al. (2012) Biol. Chem. 393:259]. The first step is to determine whether you might have a disordered protein/region:
• Does your protein’s sequence have a high ratio of charged amino acids to hydrophobic aminoacids?
• Is your protein post-translationally modified?
• Is the corresponding mRNA alternatively spliced?
• Is your protein easily proteolyzed?
• Does your protein interact with many proteins in vivo?
As an aid to biophysicists interested in exploring how disorder might contribute to the function or regulation of their protein, we will present several articles to provide some initial guidance and suggestions. If you answered “yes” to any of the above questions, this series is for you! Finally, please remember that attending the IDP subgroup meeting is an excellent way to learn about these topics and meet helpful experts in these techniques. New members are always very welcome!
—Sarah Bondos, IDP Subgroup Councilor
August 2012 Table of Contents