Basic Science and Craniofacial Biology
Room 1036, 345 E. 24th Street
Our group is focusing on lessons from Nature. The major question is: how does Nature create three-dimensional inorganic/organic based materials like sea shells, invertebrate exoskeletons, and vertebrate bone, dentine, and enamel?
As we understand it, this process uses proteins that assemble into supramolecular structures that modulate the formation of biominerals. The resulting biocomposite structure usually has modified properties as a result of protein participation. Example of unique properties include fracture and puncture resistances, amorphous precursors, single crystal formation, surface catalysis and transmission/focusing/diffusion of light.
Our ultimate goal is to determine the molecular properties of these proteins that allow matrices to assemble, mineralize, and participate in the formation of naturally-occuring organic/inorganic skeletal structures.
Solving problems at the interface of biology and materials requires knowledge of polypeptide structure, function, and how this impacts the self-assembly process and the physical properties of the biocomposite. This information can then be applied in material engineering to create new synthetic materials. The experimental aspects of our research include the use of NMR spectroscopy, SEM, TEM and AFM visualization, circular dichroism and fluorescence spectrometry, mass spectrometry, x-ray diffraction, molecular simulations, and other techniques obtained through our various collaborations.
Interested Ph.D graduates who wish to do postdoctoral research with our group are encouraged to contact us via email and provide a CV plus the names and contact info for three Ph.D advisors. Undergraduate and Graduate students from Departments of Chemistry, Biology, and NYU Medical Center can also contact us regarding joining our group as Ph.D candidates.
Department of Energy (DOE)
Complete listing available on the NYU Health Sciences Library site.
Chang, E.P., Perovic, I., Rao, A., Cölfen, H., Evans, J.S. (2016) Insect cellglycosylation and its impact on the functionality of a recombinant intracrystalline nacre protein, AP24. Biochemistry, in press.
Chang, E.P., Evans, J.S. (2015) Pif97, a von Willebrand and Peritrophin biomineralization protein, organizes mineral nanoparticles and creates intracrystalline nanochambers. Biochemistry 54, 5348-5355.
Lokappa, S., Chandrababu, B.K., Dutta, K., Perovic, I., Evans, J.S., Moradia-Oldak, J.(2015) Interactions of amelogenin with phospholipids. Biopolymers 103, 96-108.
Chang, E.P., Williamson G., Evans, J.S. (2015) Focused ion beam tomography reveals the presence of micro-, meso-, and macroporous intracrystalline regions introduced into calcite crystals by the gastropod nacre protein AP7. Crystal Growth and Design 15, 1577-1582.
Brown, A.H., Rodger, P.M., Evans, J.S., Walsh, T.R. (2015) Equilibrium conformational ensemble of the intrinsically-disordered peptide n16N: Linking sub-domain structures and function in nacre. Biomacromolecules 15, 4467-4479.
Perovic, I., Chang, E.P., Verch, A., Rao, A., Coelfen, H., Kroeger, R., Evans, J.S. (2014) An oligomeric C-RING nacre protein influences pre-nucleation events and organizes mineral nanoparticles. Biochemistry 53, 7259-7268.
Seker, U., Wilson, B., Kulp, J., Evans, J.S., Tamerler, C., Sarikaya, M. (2014) Thermodynamics of engineered gold binding peptides - Establishing the structure-activity relationships. Biomacromolecules 15, 2369-2377.
Chang, E.P., Russ, J.A., Verch, A., Kroeger, R., Estroff, L.A., Evans, J.S. (2014) Engineering of crystal surfaces and subsurfaces by an intracrystalline biomineralization protein. Biochemistry 53, 4317-4319.
Chang, E.P., Russ, J.A., Verch, A., Kroeger, R., Estroff, L.A., Evans, J.S. (2014) Engineering of crystal surfaces and subsurfaces by framework biomineralization protein phases. Cryst.Eng. Commun. 16, 7406-7409.
Perovic, I., Chang, E.P., Lui, M., Rao, A., Cölfen, H., Evans, J.S. (2014) A framework nacre protein, n16.3, self-assembles to form protein oligomers that participate in the post-nucleation spatial organization of mineral deposits. Biochemistry 53, 2739-2748.
Seto, J., Picker, A., Evans, J.S., Cölfen, H. (2014) A nacre protein sequence organizes the mineralization space for polymorph formation. Crystal Growth and Design 14, 1501-1505.
Evans, J.S. (2014) The Realities of Disordered or Unfolded Proteins: Relevance to Biomineralization. In Biomineralization Sourcebook: Characterization of Biominerals and Biomimetic Materials. Eds E. DiMasi, L.B. Gower. CRC Press, NY, NY USA.