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 en

SUBMITTER: Gronau G 

PROVIDER: S-EPMC3700428 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature