Characterization of Zinc-Histidine Interactions in Nvjp-1


Characterization of Zinc-Histidine Interactions in Nvjp-1



Brittanie M Rooths



The mandible of Nereis virens, a marine sandworm, is mostly organic with stiffness and hardness comparable to that of human dentin. Nvjp-1 is the primary protein in the Nereis jaw and is inherently Histidine rich. Histidine contributes to the stability of the protein structure and superior mechanical properties through metal-coordinate bonds. Crosslinking of purified recombinant Nvjp-1 creates a water stable hydrogel that is capable of expanding and contracting upon exposure to various ions. Nvjp-1 hydrogels exhibit sclerotization through metal-coordination with divalent cations. Over ninety percent of the amino acid sequence of the carboxy-terminal of Nvjp-1 is comprised of only four amino acids. In order to determine the genetic/protein motifs directly responsible for the mechanical response, a carboxy-terminal truncation mutant of Nvjp-1 was recombinately expressed and crosslinked to form hydrogels. Dynamic mechanical analysis was performed on the carboxy-terminal truncation mutant to compare its mechanical properties to that of the full-length protein. De Novo structure prediction was performed using Molecular Dynamics simulations as a technique for determining native protein structures. The role of Zn-Histidine interactions in Nvjp-1 and their effect on protein structure was also investigated.

Publication Date


Project Designation

Graduate Research

Primary Advisor

Rajiv Berry, Kristen Krupa Comfort

Primary Advisor's Department

Chemical Engineering


Stander Symposium project

Characterization of Zinc-Histidine Interactions in Nvjp-1