Research in the Fried Lab
Structural Proteomics Method Development
Structural proteomics is an emerging field that uses mass spectrometry in order to monitor protein structure globally, sensitively, and (in some cases) in vivo.
We focus on advancing two such methods.
Limited proteolysis mass spectrometry (LiP-MS) provides a structural snapshot of entire proteomes in a single experiment, and we have found it powerful for exploring protein refolding following denaturation, how proteins respond to physical extremes like high temperature or high pressure.
Crosslinking mass spectrometry (XL-MS) provides more detailed structural information in the form of residue-residue contacts and can also be performed in situ and rapidly (using photocrosslinkers).
Our lab develops new chemical tools, experimental workflows, and software to improve these methods and apply them to challenging system.s
Structural Proteomics of Biomolecular Condensates and Disordered Regions
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Protein Folding at the Origins of Life
Named by the Swedish biochemist Jöns Jacob Berzelius after the ancient Greek word πρώτειος (meaning ‘first’), proteins were indeed most likely the earliest biopolymer. But what were the first proteins like? Did they have access to the full modern alphabet of 20 amino acids? (Probably not). Could they have been able to fold and function even in the absence of nucleic acids to encode them? (We think yes). Our lab interrogates the biophysics of prebiotically plausible proteins and peptides. to test what roles they might have played at the earliest stages of life’s emergence.
Exploring Protein Folding from the Proteome-wide perspective
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The Molecular Basis of Aging and Cognitive Decline
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