title: Effect of sodium chloride on the structure and stability of spider silk's N-terminal protein domain.
abstract: A spider's ability to store silk protein solutions at high concentration is believed to be related to the protein's terminal domains. It has been suggested that a shift in salt concentration and pH can have a significant influence on the assembly process. Based on experimental data, a model has been proposed in which the N-terminal domain exists as a monomer during storage and assembles into a homodimer upon spinning. Here we perform a systematic computational study using atomistic, coarse-grained and well-tempered metadynamics simulation to understand how the NaCl concentration in the solution affects the N-terminal domain of the silk protein. Our results show that a high salt concentration, as found during storage, weakens key salt bridges between the monomers, inducing a loss in bond energy by 28.6% in a single salt bridge. As a result dimer formation is less likely as 35.5% less energy is required to unfold the dimer by mechanical force. Conversely, homodimer formation appears to be more likely at low salt concentrations as the salt bridge stays at the lower energy state. The link between salt concentration, structure and stability of the N-terminal domain provides a possible mechanism that prevents premature fiber formation during storage.
authors.affiliation: Laboratory for Atomistic and Molecular Mechanics (LAMM), Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, 77 Mass. Ave. Room 1-235A&B, Cambridge, MA 02139, USA ; Institute for Particle Technology, Technische Universität Braunschweig, Volkmaroder Str. 5, 38104 Braunschweig, Germany.
authors.forename: Greta
authors.initials: G
authors.lastname: Gronau
authors.forename: Zhao
authors.initials: Z
authors.lastname: Qin
authors.forename: Markus J
authors.initials: MJ
authors.lastname: Buehler
keywords: Salt bridge; assembly; coarse-grained model; free-energy landscape; metadynamics; molecular dynamics; nanomechanics; spidroin