title: FoldEco: a model for proteostasis in E. coli.
abstract: To gain insight into the interplay of processes and species that maintain a correctly folded, functional proteome, we have developed a computational model called FoldEco. FoldEco models the cellular proteostasis network of the E. coli cytoplasm, including protein synthesis, degradation, aggregation, chaperone systems, and the folding characteristics of protein clients. We focused on E. coli because much of the needed input information--including mechanisms, rate parameters, and equilibrium coefficients--is available, largely from in vitro experiments; however, FoldEco will shed light on proteostasis in other organisms. FoldEco can generate hypotheses to guide the design of new experiments. Hypothesis generation leads to system-wide questions and shows how to convert these questions to experimentally measurable quantities, such as changes in protein concentrations with chaperone or protease levels, which can then be used to improve our current understanding of proteostasis and refine the model. A web version of FoldEco is available at http://foldeco.scripps.edu.
authors.affiliation: Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USA. epowers@scripps.edu
authors.forename: Evan T
authors.initials: ET
authors.lastname: Powers
authors.forename: David L
authors.initials: DL
authors.lastname: Powers
authors.forename: Lila M
authors.initials: LM
authors.lastname: Gierasch
mesh_terms: D019295:Computational Biology / Q000379:methods*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D020407:Internet; D007700:Kinetics; D008954:Models, Biological; D014176:Protein Biosynthesis; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D059748:Proteolysis; D020543:Proteome / Q000378:metabolism*; D012984:Software; D013379:Substrate Specificity
chemical_list: D029968:Escherichia coli Proteins; D020543:Proteome