Biophysical studies support our hypothesis. Biochemistry, 56 35 When the maltose triggering agent was removed, the degradation of the antibiotic instantly slowed to its original pace.
Through the Johns Hopkins Technology Transfer office, Ostermeier and Chapman Wright have filed for patent protection covering the protein switch for cancer technology.
Code is available here: Ostermeier believed a very small number of these new fusion proteins might possess the molecular switch behavior he was looking for. Hilser Ligand Effects on the protein ensemble: When we introduce this switch into bacteria, it transforms them into a working sensor.
Analysis of the Native State Ensemble.
Beta-lactamase is an enzyme that can disable and degrade penicillin-like antibiotics. Marc Ostermeier is an assistant professor in the Department of Chemical and Biomolecular Engineering.
However, targeted MTases require clear design rules to direct site-specific DNA methylation and minimize the unintended effects of off-target DNA methylation.
This series of fitness and epistatic landscapes provided extensive experimental insight into the relationships between mutation, protein structure, protein stability, and epistasis and revealed the tradeoffs inherent in the evolution of new functions. A comparison of Existing Models and Further Analysis.
They also might be used to set off a warning signal when biological warfare agents are present. The second then carries out the task.
Hilser Energetic Profiling of Protein Folds. Thus, the work demarcates an important physiological constraint that shapes the efficiency of the system and one to take into account as we think about novel ways of improving photosynthesis. Similarly coupled proteins may someday be used to produce specialized molecules that deliver lethal drugs only to cancerous cells.
First, it is possible to create protein switches by domain insertion using input domains that do not undergo large conformational changes upon ligand binding.
In Protein Dynamics pp. A large portion of her thesis work was published in July in Scientific Reportswith a follow up paper soon to be submitted. Structural and energetic basis of allostery.Awards & Honors.
Faculty Awards. Thermodynamics of Water Modeled with Ab Initio Simulations” in The Journal of Chemical Physics, a top-downloaded paper published in October of Honorable Mentions were awarded to Barrett Steinberg and Nathan Nicholes of the Ostermeier lab and. Co-authors on the paper were Ostermeier, Eshleman and R.
Clay Wright (not related to Chapman Wright), a doctoral student in Ostermeier’s lab. Through the Johns Hopkins Technology Transfer office, Ostermeier and Chapman Wright have filed for patent protection covering the protein switch for cancer technology. Gurkan Guntas, a doctoral student in Ostermeier's lab, was lead author on the new Chemistry & Biology paper.
The co-authors were Ostermeier and Sarah F. Mitchell, a doctoral student in the Program. A Mudd Hall Department of Biology Johns Hopkins University N. Charles Street Baltimore, MD Email: [email protected] Office In lab tests, the researchers showed that these switches, working from inside the cells, can activate a powerful cell-killing drug when the device detects a marker linked to cancer.
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