The Noyes Lab
The Noyes Lab 2.0, not to be confused with the Princeton 1.0 version, started at the NYU School of Medicine in the summer of 2015. We are interested in how proteins interact with their targets from structural, computational and cell biology perspectives. As such, our primary goals involve developing new tools to sample these interactions as comprehensively as possible. Our research could be classified as Systems or Synthetic Biology but we hope not to lose sight of the Cell Biology that this is all predicated upon.
I also like to think we are a fun group of people with a diverse set of interests, both in and out of the lab. My hope is that we are creating an enthusiastic, energetic, and friendly atmosphere; and that the Noyes lab becomes known as a special environment to train young scientists for the careers they desire.
Welcome April Mueller who transitions from undergraduate to Research Scholar/Technician in the lab!
Congratulations to David Ichikawa, recipient of T32 funding from the Molecular Pharmacology training grant! Nice work David.
Congratulations to April Mueller who not only graduates Summa Cum Laude AND with departmental honors in Chemistry....but she also won the George Granger Brown Scholarship Award AND the Herold Seidenstein Award in Chemistry! Amazing work from an amazing undergraduate!
***Graduate Student and Postdoctoral positions available. Please feel free to contact me directly.
Bio, Marcus Noyes PhD
Dr. Marcus Noyes joined the NYU Institute for Systems Genetic and the Department of Biochemistry and Molecular Pharmacology in July of 2015. Dr. Noyes received his PhD from the University of Massachusetts Medical School where he developed tools for the high-throughput characterization of protein-DNA interactions. He was next recruited as an independent Lewis-Sigler Fellow at Princeton University where he ran a small lab for 5 years before accepting his current position at NYU. His research rests on the edge of Systems and Synthetic Biology, focusing on the development of tools that allow us to understand the binding potential of common protein domains important for biological functions. Using comprehensive, synthetic screens of these protein domains, the goal of his research is to understand the complete functional capacity of a protein and not be limited by the sometimes small set of functions that have evolved. This approach has the added benefit of producing new proteins with novel functions that can be applied to therapeutic applications such as protein inhibition and precise genome editing.