Crystal Stackhouse

All Publications

• Characterization of 10MAG/LDAO reverse micelles: Understanding versatility for protein encapsulation. Biophysical chemistry Stackhouse, C. I., Pierson, K. N., Labrecque, C. L., Mawson, C., Berg, J., Fuglestad, B., Nucci, N. V. 2024; 311: 107269

  Abstract

  Reverse micelles (RMs) are spontaneously organizing nanobubbles composed of an organic solvent, surfactants, and an aqueous phase that can encapsulate biological macromolecules for various biophysical studies. Unlike other RM systems, the 1-decanoyl-rac-glycerol (10MAG) and lauryldimethylamine-N-oxide (LDAO) surfactant system has proven to house proteins with higher stability than other RM mixtures with little sensitivity to the water loading (W0, defined by the ratio of water to surfactant). We investigated this unique property by encapsulating three model proteins - cytochrome c, myoglobin, and flavodoxin - in 10MAG/LDAO RMs and applying a variety of experimental methods to characterize this system's behavior. We found that this surfactant system differs greatly from the traditional, spherical, monodisperse RM population model. 10MAG/LDAO RMs were discovered to be oblate ellipsoids at all conditions, and as W0 was increased, surfactants redistributed to form a greater number of increasingly spherical ellipsoidal particles with pools of more bulk-like water. Proteins distinctively influence the thermodynamics of the mixture, encapsulating at their optimal RM size and driving protein-free RM sizes to scale accordingly. These findings inform the future development of similarly malleable encapsulation systems and build a foundation for application of 10MAG/LDAO RMs to analyze biological and chemical processes under nanoscale confinement.

  View details for DOI 10.1016/j.bpc.2024.107269

  View details for PubMedID 38815545

• Impacts of HIV-1 5′ UTR structure on mRNA translation initiation Stackhouse, C. I., Jackson, L. N., Alvarado, C., Grosely, R., Puglisi, J. D., Puglisi, E. CELL PRESS. 2024: 360A-361A

  View details for Web of Science ID 001194120702165

• Probing hydration dynamics of antifreeze protein M1.1 by NMR spectroscopy Zangaro, J. T., Stackhouse, C. I., Nucci, N. V. CELL PRESS. 2024: 352A-353A

  View details for Web of Science ID 001194120702126