University of California, Riverside

Department of Chemistry

Chemical Sciences

chemical biologyResearch in Chemical Biology at UC Riverside spans a broad area at the Chemistry-Biology interface. The central focus is to develop and apply chemical techniques and tools to study and manipulate biological systems. Research directions include combinatorial chemistry, laboratory engineering of proteins and nucleic acids, DNA damage and mutagenesis, optical and electrochemical biosensors, theoretical and experimental studies on biological dynamics and interactions, spectroscopic characterization of biosystems, and structural biology of biomolecules. Active collaborations exist within the Chemistry Department, as well as with research groups in other departments such as Biochemistry, Cell Biology and Neuroscience, Botany and Plant Science, Entomology, and Institute for Integrative Genome Biology. Please follow the links below to learn more about the individual Chemical Biology research groups at UCR.

Graduate students with a focus in Chemical Biology are expected to receive broad and highly interdisciplinary trainings in bioanalytical, bioorganic and biophysical chemistry.

Faculty Research Description:

Chia-en Chang
Molecular dynamics in chemical and biological systems: The Chang group primarily uses computational methods to investigate the chemistry of biological systems. The goal is to understand how molecules can bind and how molecular flexibility influences ligand binding, and use the knowledge to design drugs and interpret experiments. We have developed new methods to understand ligand binding kinetics.

Quan Jason Cheng
Research in the Cheng lab focuses on bio- and chemical sensors, functional biomaterials, and label-free surface plasmon resonance (SPR) techniques. We are particularly interested in measurement techniques involving supported lipid membranes, protein microarrays, surface-assisted MS methods, and novel platforms allowing orthogonal detection.

Joseph Genereux
The Genereux lab develops and applies mass spectrometry-based proteomic techniques that can elucidate molecular mechanisms of lipoprotein folding, assembly, misfolding, and protein homeostasis. By integrating these with in situ analytical approaches, we generate biological hypotheses that are then investigated using molecular and cellular biology.  

Richard Hooley
Synthetic Organic, Inorganic and Supramolecular chemistry. Our projects include: the synthesis of biomimetic supramolecular constructs capable of selective molecular recognition; synthesis of new water-soluble catalysts and host molecules; dynamic NMR studies of host:guest interactions; biosensors based on synthetic receptor molecules.

Ryan Julian
Protein homoeostasis is vital for proper cellular function and involves the turnover, or recycling of proteins. Although many proteins exist briefly, with half-lives of less than 48 hours, other proteins persist for years or longer. In some systems, such as the lens of the eye, proteins never turnover and must remain viable for the entire lifetime of an organism. Degradation of these long-lived proteins occurs in various ways including truncation, misfolding, and post-translational modification. Furthermore, degradation can be spontaneous or enzymatically driven. Many of these processes interact and influence each other, and, in the end, misbehavior of long-lived proteins eventually leads to malfunction and even cell death. We are interested in characterizing the relationships between the properties, structures, and functions of long-lived proteins utilizing mass spectrometry and other related techniques.

Leonard Mueller
Solid-state and solution-state NMR as a probe of structure and dynamics.

Michael Pirrung
Chemical biology, synthetic organic chemistry, nucleic acids, combinatorial chemistry; photochemistry.

Timothy Su

Christopher Switzer
Design, synthesis and characterization of nucleic acid variants with new properties for molecular recognition, catalysis and replication.

Yinsheng Wang
Chemistry and biology of DNA damage, quantitative proteomics. A multi-pronged approach, encompassing synthetic chemistry, mass spectrometry-based bioanalytical chemistry, biochemistry and molecular biology, is employed to understand at the molecular level how structurely defined DNA lesions are repaired and how they compromise the flow of genetic information during DNA replication and transcription. Quantitative proteomics method is used for understanding the molecular mechanisms of action of anticancer drugs and environmental toxicants.

Min Xue
The Xue group studies peptides that are capable of supramolecular recognition. When coupled with spectroscopy and microscopy, these peptides provide the basis to a series of bioanalytical methods. The long term goal is to use these methods to better understand the cell signaling pathways and develop novel therapeutics.

Linlin Zhao

The overarching goal of our research is to decipher the mechanisms of mitochondrial DNA turnover and repair and clarify their roles in mitochondrial pathogenesis. We combine mass spectrometry-based bioanalytical approaches with protein biochemistry, mechanistic enzymology, and cellular approaches to gain quantitative insights into the mitochondrial DNA maintenance process. We envision that the new knowledge from our research will further the understanding of mitochondrial pathology and inform the development of novel therapeutics for mitochondrial diseases.

Wenwan Zhong
Advancement and applications of separation technologies in study of ligand-receptor interaction and protein complex formation; Signal amplification and on-chip sample processing for detection of disease markers; Preparation of bionanomaterials for sensing and biomolecule preconcentration.

More Information 

General Campus Information

University of California, Riverside
900 University Ave.
Riverside, CA 92521
Tel: (951) 827-1012

Department Information

Department of Chemistry
Chemical Sciences
501 Big Springs Road

Tel: (951) 827-3789 (Chair's Assistant)
Fax: (951) 827-2435 (confidential)