Roy Zhao

All Publications

• SOFIA/HAWC plus Far-infrared Polarimetric Large Area CMZ Exploration Survey. V. The Magnetic Field Strength and Morphology in the Sagittarius C Complex ASTROPHYSICAL JOURNAL Zhao, R. J., Morris, M. R., Chuss, D. T., Pare, D. M., Guerra, J. A., Butterfield, N. O., Wollack, E. J., Karpovich, K. 2025; 988 (2)

  View details for DOI 10.3847/1538-4357/ade80d

  View details for Web of Science ID 001539919600001

• SOFIA/HAWC plus Far-infrared Polarimetric Large-area CMZ Exploration Survey. IV. Relative Magnetic Field Orientation throughout the CMZ ASTROPHYSICAL JOURNAL Pare, D. M., Chuss, D. T., Karpovich, K., Butterfield, N. O., Iuliano, J., Pan, X., Wollack, E. J., Zhang, Q., Morris, M. R., Nilsson, M., Zhao, R. J. 2025; 978 (1)

  View details for DOI 10.3847/1538-4357/ad9586

  View details for Web of Science ID 001382143000001

• A High-Throughput Workflow to Analyze Sequence-Conformation Relationships and Explore Hydrophobic Patterning in Disordered Peptoids. Chem Day, E. C., Chittari, S. S., Cunha, K. C., Zhao, R. J., Dodds, J. N., Davis, D. C., Baker, E. S., Berlow, R. B., Shea, J. E., Kulkarni, R. U., Knight, A. S. 2024; 10 (11): 3444-3458

  Abstract

  Understanding how a macromolecule's primary sequence governs its conformational landscape is crucial for elucidating its function, yet these design principles are still emerging for macromolecules with intrinsic disorder. Herein, we introduce a high-throughput workflow that implements a practical colorimetric conformational assay, introduces a semi-automated sequencing protocol using MALDI-MS/MS, and develops a generalizable sequence-structure algorithm. Using a model system of 20mer peptidomimetics containing polar glycine and hydrophobic N-butylglycine residues, we identified nine classifications of conformational disorder and isolated 122 unique sequences across varied compositions and conformations. Conformational distributions of three compositionally identical library sequences were corroborated through atomistic simulations and ion mobility spectrometry coupled with liquid chromatography. A data-driven strategy was developed using existing sequence variables and data-derived 'motifs' to inform a machine learning algorithm towards conformation prediction. This multifaceted approach enhances our understanding of sequence-conformation relationships and offers a powerful tool for accelerating the discovery of materials with conformational control.

  View details for DOI 10.1016/j.chempr.2024.07.025

  View details for PubMedID 39582487

  View details for PubMedCentralID PMC11580747

• Dust in high-redshift galaxies: reconciling UV attenuation and IR emission JOURNAL OF COSMOLOGY AND ASTROPARTICLE PHYSICS Zhao, R. J., Furlanetto, S. R. 2024

  View details for DOI 10.1088/1475-7516/2024/09/018

  View details for Web of Science ID 001312415100013

• Insights into conformational ensembles of compositionally identical disordered peptidomimetics. Polymer chemistry Day, E. C., Cunha, K. C., Zhao, R. J., DeStefano, A. J., Dodds, J. N., Yu, M. A., Bemis, J. R., Han, S., Baker, E. S., Shea, J. E., Berlow, R. B., Knight, A. S. 2024; 15 (29): 2970-2980

  Abstract

  While the conformational ensembles of disordered peptides and peptidomimetics are complex and challenging to characterize, they are a critical component in the paradigm connecting macromolecule sequence, structure, and function. In molecules that do not adopt a single predominant conformation, the conformational ensemble contains rich structural information that, if accessible, can provide a fundamental understanding related to desirable functions such as cell penetration of a therapeutic or the generation of tunable enzyme-mimetic architecture. To address the fundamental challenge of describing broad conformational ensembles, we developed a model system of peptidomimetics comprised of polar glycine and hydrophobic N-butylglycine to characterize using a suite of analytical techniques. Using replica exchange molecular dynamics atomistic simulations and liquid chromatography coupled to ion mobility spectrometry, we were able to distinguish the conformations of compositionally identical model sequences. However, differences between these model sequences were more challenging to resolve with characterization tools developed for intrinsically disordered proteins and polymers, including double electron-electron resonance (DEER) spectroscopy and diffusion ordered spectroscopy (DOSY) NMR. Finally, we introduce a facile colorimetric assay using immobilized sequences that leverages a solvatochromic probe, Reichardt's dye, to visually reveal conformational trends consistent with the experimental and computational analysis. This rapid colorimetric technique provides a complementary method to characterize the disorder of macromolecules and examine conformational ensembles as an isolated or multiplexed technique.

  View details for DOI 10.1039/D4PY00341A

  View details for PubMedID 39781370

  View details for PubMedCentralID PMC11709448