Researchers develop a method to investigate how bacteria respond to starvation and to identify which proteins bind to the "magic spot" - ppGpp.
Image Credit:Geoff Fudenberg and Leonid Mirny
Research in Molecular Biophysics and Structural Biology at MIT studies fundamental properties of molecules and systems, often by integrating computational thinking, engineering designs, and biophysical insights.
New approach generates a wider variety of protein sequences optimized to bind to drug targets.
Designing synthetic proteins that can act as drugs for cancer or other diseases can be a tedious process: It generally involves creating a library of millions of proteins, then screening the library to find proteins that bind the correct target.
Thanks to continued advances in genetic sequencing, scientists have identified virtually every A, T, C, and G nucleotide in our genetic code. But to fully understand how the human genome encodes us, we need to go one step further, mapping the function of each base.
MIT Professor sees many "big, deep questions in biology" that benefit from study by both physicists and life scientists.
It’s a pretty good bet that among MIT’s physics faculty, Jeff Gore is the only one with test tubes of yeast growing in his lab.
Gore, a biophysicist who studies population dynamics, uses yeast and other microbes to explore the fundamental rules that govern phenomena such as population collapse. His microbial communities offer a window into principles that also influence larger-scale populations that are much more difficult to study.
New discovery suggest that all life may share a common design principle.
New finding suggests differences in how humans and bacteria control production of DNA's building blocks.
Using a state-of-the-art type of electron microscopy, an MIT-led team has discovered the structure of an enzyme that is crucial for maintaining an adequate supply of DNA building blocks in human cells.
Student: Vincent Xue
Title: Modeling and Designing Bcl-2 Family Protein Interactions Using High-Throughput Interaction Data
Drug that targets a key cancer protein could combat leukemia and other types of cancer.
MIT biologists have designed a new peptide that can disrupt a key protein that many types of cancers, including some forms of lymphoma, leukemia, and breast cancer, need to survive.
The new peptide targets a protein called Mcl-1, which helps cancer cells avoid the cellular suicide that is usually induced by DNA damage. By blocking Mcl-1, the peptide can force cancer cells to undergo programmed cell death.
An abundant enzyme in marine microbes may be responsible for production of the greenhouse gas.