Stabilization of Proteins in Confined Spaces

Citations Over TimeTop 10% of 2001 papers

Abstract

We present theory showing that confining a protein to a small inert space (a "cage") should stabilize the protein against reversible unfolding. Examples of such spaces might include the pores within chromatography columns, the Anfinsen cage in chaperonins, the interiors of ribosomes, or regions of steric occlusion inside cells. Confinement eliminates some expanded configurations of the unfolded chain, shifting the equilibrium from the unfolded state toward the native state. The partition coefficient for a protein in a confined space is predicted to decrease significantly when the solvent is changed from native to denaturing conditions. Small cages are predicted to increase the stability of the native state by as much as 15 kcal/mol. Confinement may also increase the rates of protein or RNA folding.

Related Papers

• → Is protein folding hierarchic? II. Folding intermediates and transition states(1999)383 cited
• → Improving folding properties of computationally designed proteins(2019)8 cited
• → Reshaping the Protein Folding Pathway by Osmolyte via its Effects on the Folding Intermediates(2015)10 cited
• → Biosynthetic Protein Folding and Molecular Chaperons(2022)4 cited
• → Using Single-Molecule Chemo-Mechanical Unfolding to Simultaneously Probe Multiple Structural Parameters in Protein Folding(2019)