Multiplexed method reveals protein energy landscapes across 10 domain families
What to know about Multiplexed method reveals protein energy landscapes across 10 domain families
Scientists at Northwestern Medicine have developed a new experimental method called multiplexed hydrogen-deuterium exchange mass spectrometry (mHDX-MS) to analyze protein energy landscapes at scale. The study, published in Nature, allows for the parallel analysis of thousands of protein sequences to better understand how conformational fluctuations relate to protein function and disease.
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What happened
Multiplexed method reveals protein energy landscapes across 10 domain families Gaby Clark Scientific Editor Robert Egan Associate Editor Northwestern Medicine scientists have developed a new experimental method to analyze conformational fluctuations in…
Why it matters
"Proteins move around between different structures but understanding what the energies of those different conformations are and how rare or common those conformations is totally unknown for most proteins.
Common ground
This study was really about developing a new method that let us illuminate all these different dynamics of proteins on a large scale for the first time," said Gabriel Rocklin, Ph.D., assistant professor of Pharmacology, who was senior author of the study.
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Scientists at Northwestern Medicine have developed a new experimental method called multiplexed hydrogen-deuterium exchange mass spectrometry (mHDX-MS) to analyze protein energy landscapes at scale. The study, published in Nature, allows for the parallel analysis of thousands of protein sequences to better understand how conformational fluctuations relate to protein function and disease.
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fact_checkClaims Checked
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