2011/06/01 by Joseph A. Marsh, Joseph A. Marsh, Sarah A. Teichmann +1 · 1 citation
Biochemistry, Genetics and Molecular Biology · Chemistry · Materials Science · #Enzyme Structure and Function #Mass Spectrometry Techniques and Applications #Protein Structure and Dynamics
paper · pdf · doi:10.1016/j.str.2011.03.010
openalex publication_date 2011/06/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/04
Protein interactions are often accompanied by significant changes in conformation. We have analyzed the relationships between protein structures and the conformational changes they undergo upon binding. Based upon this, we introduce a simple measure, the relative solvent accessible surface area, which can be used to predict the magnitude of binding-induced conformational changes from the structures of either monomeric proteins or bound subunits. Applying this to a large set of protein complexes suggests that large conformational changes upon binding are common. In addition, we observe considerable enrichment of intrinsically disordered sequences in proteins predicted to undergo large conformational changes. Finally, we demonstrate that the relative solvent accessible surface area of monomeric proteins can be used as a simple proxy for protein flexibility. This reveals a powerful connection between the flexibility of unbound proteins and their binding-induced conformational changes, consistent with the conformational selection model of molecular recognition.