Marcey Waters

Marcey Waters

Glen H. Elder, Jr. Distinguished Professor, Co-Chair of Diversity

   Caudill Laboratories 219
  Group Website
  Curriculum Vitae

Research Interests

Bioorganic Chemistry, Molecular Recognition

Research Synopsis

Our group is an interdisciplinary group, focusing on problems of molecular and biomolecular recognition. Molecular recognition impacts a wide range of fields, including asymmetric catalysis, materials chemistry, and protein folding. Consider, for example, designing a drug to bind to the active site of an enzyme. What features other than shape might contribute to binding? What types of interactions will provide high affinity as well as high selectivity? These are general questions in the field of molecular recognition that we are investigating for applications to biosensing, drug delivery, and de novo protein design.
The research interests in our group span a wide range, from mechanistic organic chemistry and molecular recognition to structural biology, and hence involve the use of a variety of techniques. Methods used in our group include organic and solid phase synthesis, combinatorial chemistry, computational chemistry, molecular biology, kinetic and thermodynamic measurements using 1D and 2D NMR, circular dichroism, UV/Vis and fluorescence spectroscopy, analytical ultracentrifugation, and calorimetry. The extent that any one student uses these techniques depends largely on the particular student's research interests.

Professional Background

BA, UCSD, 1992; PhD, The University of Chicago, 1997; NIH Postdoctoral Fellow, Columbia University, 1997-1999; NSF Career Award, 2001-2006; Alfred P. Sloan Fellow, 2004-2006; Board of Directors, Mesilla Chemistry Workshop; Advisory Board Member, International Symposia on Macrocyclic and Supramolecular Chemistry.

Research Group

News & Publications

This study describes the development of a two-pronged approach combining genetic code expansion (GCE) and structure–activity relationships (SAR) through systematic variation of both the aromatic binding pocket in the protein and the alkyllysine residues in the peptide to probe inhibitor recognition in the CBX5 chromodomain.


The UNC Eshelman School of Pharmacy is joining forces with the UNC Department of Chemistry to establish an NIH-funded UNC Chemistry-Biology Interface Training Program that will support graduate students preparing for careers in modern biomedical science.