Levels of regulation of protein bioconformatics can be manipulated to commercial advantage.

manipulation of heterogeneity in cis and trans

A nascent secretory/integral membrane protein chain emerges in the cytoplasm (I).
Mechanisms exist (including perhaps, as indicated, cytoplasmic binding proteins, II) by which the nascent chain is directed to the ER membrane (III), such that the translocon is organized differently. As a result of differences in translocon organization, and consequent differences in protein-protein interactions (III), an initially homogeneous population of nascent chains is directed down different folding funnels (IV,) such that the final folded shape/transmembrane topology are different (conformers, V). In vivo there may be multiple mechanisms to achieve translocon reorganization and its consequent change in conformer distribution (e.g. different binding proteins, activation of different signaling pathways). In vivo this heterogeneity is particularly difficult to detect because some conformers will be rapidly degraded, except when needed by the cell. Prosetta's science involves elucidating conformer structure and function and manipulation of those characteristics for commercial advantage.