title: Macromolecular mechanisms of protein translocation.
abstract: When macromolecules such as proteins are forced to translocate through a narrow pore, their conformational entropy is reduced, resulting in a free energy barrier. This free energy barrier is additionally modulated by protein-pore interactions. Furthermore, the driving force of the translocation such as the electrochemical potential gradient and electroosmotic flow navigates the transport of the protein through the free energy landscape. Depending on the specifics of the protein-pore system and the driving force, the details of the translocation process and their statistical properties such as the average translocation time can vary significantly. Nevertheless, there are a few fundamental physical concepts that underly the ubiquitous phenomenon of polymer translocation, which are reviewed here.
authors.affiliation: Department of Polymer Science and Engineering, University of Massachusetts, Amherst, MA 01003, USA. muthu@polysci.umass.edu.
authors.forename: M
authors.initials: M
authors.lastname: Muthukumar
mesh_terms: D000818:Animals; D019277:Entropy; D006801:Humans; D058608:Nanopores / Q000648:ultrastructure; D011487:Protein Conformation; D021381:Protein Transport; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D011506:Proteins