Bryan Wilkins

Assistant Professor, Chemistry & Biochemistry

I have a passion for biological chemistry with a particular interest in the field of synthetic biology. This growing discipline combines facets of biology, chemistry and engineering, and can be used to manipulate and redesign existing biological systems for useful purposes. I utilize a technique that has engineered the natural components of protein translation to introduce “unnatural amino acids” into protein. Unnatural amino acids are chemically synthesized to possess altered R-groups providing unique chemical handles with which to query biologically relevant molecular interactions at the protein level. 

Throughout my scientific career I have been intimately involved in teaching and mentoring students. This has included positions such as teaching assistant, adjunct professor, research supervisor and now assistant professor. I have always maintained a great fondness for instructing and enjoy transferring my love of science to my students.


2004-2010  Ph.D., University of Maryland, College Park, Maryland

1999-2003  B.S., Elizabethtown College, Elizabethtown, Pennsylvania

Courses Taught

CHEM 436, Biochemistry Laboratory

CHEM 457, Biochemistry III, Biochemistry of Nucleic Acids

CHEM 459, Biochemistry III Laboratory

CHEM 460, Chemical Research

CHEM 101, General Chemistry I

CHEM 102, General Chemistry II

  • Research

    The storage of genetic information within DNA sequences is the underlying code that defines an organism and it’s function. Genomic integrity is dependent upon the faithful replication and maintenance of DNA. Not only must the cell coordinate standard processes essential for gene transcription, DNA replication, and division, but it must also deliver rescue mechanisms in response to DNA damaging agents. 

    Histone posttranslational modifications (PTMs) play an essential regulatory role in all aspects of chromatin function. Each of the core histones is vastly decorated with different PTMs, altering the side-chain chemistry and influencing changes in histone-DNA and histone-protein interactions. The chromatin landscape is shaped by an immense field of histone PTM writers, readers, and erasers. It is the concise balance of each of these factors that conserves chromatin plasticity and permits the fluid chromatin dynamics essential for proper function.

    There remains an insufficient amount of data regarding the complicated molecular interactions that occur on the nucleosomal surface, particularly in the context of the living cell. My interests are focused on the subtleties of histone proteins and how their modifications influence chromatin architecture and molecular contacts that occur on the nucleosome. With the techniques we have established, we can now investigate the impact of histone PTMs in all aspects of chromatin biology as well as begin to illuminate the substantial interactome required for proper genome stability and integrity. 

    To address chromatin function and structure in living cells we exploit a synthetic biology technique that allows for the expansion of the genetic code in Saccharomyces cerevisiae. This system requires an evolved tRNA/aminoacyl-tRNA synthetase pair that act as orthogonal cellular components to encode for unnatural amino acids in response to an amber stop codon. The recombinant expression of these orthogonal pieces allow for a wide assortment of non-native chemistries to be introduced at the genetic level.

    In particular we are interested in the amino acid, p-benzoylphenylalanine. It contains a photo-inducible chemical crosslinking side chain that allows us to capture and monitor protein-protein interactions in vivo. We genetically encode this UAA into histone proteins and scan the nucleosomal surface for binding partners. We aim to expose nucleosomal protein-protein interactions and the mechanistic details of chromatin dynamics in yeast.

  • Publications and Scholarly Activities

    Bryan J. Wilkins, Liljan E. Hahn, Svenja Heitmüller, Holm Frauendorf, Oliver Valerius, Gerhard Braus and Heinz Neumann. Genetically encoding lysine modifications on histone H4. ACS Chem Biol. 2015, 10 (4): 939-944.

    Bryan J. Wilkins, Nils A. Rall, Yogesh Ostwal, Tom Kruitwagen, Kyoko Hiragami-Hamada, Marco Winkler, Yves Barral, Wolfgang Fischle and Heinz Neumann. A cascade of histone modifications induces chromatin condensation in mitosis. Science. 2014, 343: 77-80. 

  • Professional Experience and Memberships

    2015-           Assistant Professor, Department of Chemistry and Biochemistry, Manhattan College

    2010-2015  Postdoctoral Fellow, University of Göttingen, Germany

  • Honors, Awards, and Grants

    Alexander von Humboldt Fellow

    Göttingen Center for Molecular Biology Postdoctoral Research Award

    Drs. Wayne T. and Mary T. Hockmeyer Endowed Fellowship