Communication: folding of glycosylated proteins under confinement.
Conjugating flexible polymers (such as oligosaccharides) to proteins or confining a protein in a restricted volume often increases protein thermal stability. In this communication, we investigate the interplay between conjugation and confinement which is not trivial as the magnitude and the mechanism of stabilization are different in each instance. Using coarse-grained computational approach the folding biophysics is studied when the protein is placed in a sphere of variable radius and is conjugated to 0-6 mono- or penta-saccharides. We observe a synergistic effect on thermal stability when short oligosaccharides are attached and the modified protein is confined in a small cage. However, when large oligosaccharides are added, a conflict between confinement and glycosylation arises as the stabilizing effect of the cage is dramatically reduced and it is almost impossible to further stabilize the protein beyond the mild stabilization induced by the sugars.
Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel.
Dalit
D
Shental-Bechor
Yaakov
Y
Levy
D006023:Glycoproteins / Q000737:chemistry*; D006031:Glycosylation; D009844:Oligosaccharides / Q000737:chemistry; D017510:Protein Folding; D055550:Protein Stability; D013816:Thermodynamics
D006023:Glycoproteins; D009844:Oligosaccharides