title: Variable interactions between protein crowders and biomolecular solutes are important in understanding cellular crowding.
abstract: The effect of cellular crowding was examined from molecular dynamics simulations of chymotrypsin inhibitor 2 (CI2) in the presence of either lysozyme or bovine serum albumin (BSA) crowder molecules as a complement to recent experimental studies of the same systems (Miklos, A. C.; Sarkar, M.; Wang, Y.; Pielak, G. J. J. Am. Chem. Soc.2011, 133, 7116). The simulations confirm a destabilization and significantly slowed diffusion of CI2 in the presence of lysozyme and indicate that this observation is a result of extensive, nonspecific protein-protein interactions between CI2 and lysozyme. CI2 interacts much less with BSA crowders corresponding to a weak effect of crowding. Energetic analysis suggests an overall favorable crowding free energy in the presence of lysozyme, while weaker interactions with BSA appear to be unfavorable.
authors: Department of Biochemistry & Molecular Biology, Michigan State University, East Lansing, Michigan 48824, United States. feig@msu.edu
authors: Michael
authors: M
authors: Feig
authors: Yuji
authors: Y
authors: Sugita
mesh_terms: D000818:Animals; D002417:Cattle; D009113:Muramidase / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D025941:Protein Interaction Mapping; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D010455:Peptides; D010940:Plant Proteins; C093336:chymotrypsin inhibitor 2; D012710:Serum Albumin, Bovine; D009113:Muramidase