A new crosslinking mass spectrometry technology for studying conformational and structural changes in protein complexes

Our work describing a new crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and proteins complexes has been published in eLife.

A new crosslinking mass spectrometry technology for studying conformational and structural changes in protein complexes
A new crosslinking mass spectrometry technology for studying conformational and structural changes in protein complexes

A Better Understanding of DNA Unpacking

Jie Luo and Jeff Ranish collaborated on a project to determine the molecular architecture of the NuA4/Tip60 co-activator complex. This protein complex functions to allow proper control of gene expression and DNA repair by allowing other proteins to access the DNA in the cell nucleus. The new information about the structure and function of TIP60 could provide insight into different diseases where the protein complex plays a role, such as Alzheimer’s and various cancers. The work was published in Science.

A Better Understanding of DNA Unpacking
A Better Understanding of DNA Unpacking

Ranish lab published a preprint describing a new crosslinking mass spectrometry technology

Dynamic conformational and structural changes in proteins and protein complexes play a central and ubiquitous role in the regulation of protein function, yet it is very challenging to study these changes, especially for large protein complexes, under physiological conditions. To address this challenge, we created a novel isobaric crosslinker, Qlinker, for studying conformational and structural changes in proteins and protein complexes using quantitative crosslinking mass spectrometry (qCLMS).

Ranish lab published a preprint describing a new crosslinking mass spectrometry technology
Ranish lab published a preprint describing a new crosslinking mass spectrometry technology

Identification of key residues within p52/Tfb2 required for TFIIH function at transcription start sites in human and yeast cells

Completing a years-long collaboration with the Taatjes and Kaplan labs, we publish an article in JBC that identifies key residues within the p52/Tfb2 subunit that control TFIIH function at transcription start sites in human and yeast cells.

Identification of key residues within p52/Tfb2 required for TFIIH function at transcription start sites in human and yeast cells
Identification of key residues within p52/Tfb2 required for TFIIH function at transcription start sites in human and yeast cells
Dr. Jeff Ranish and Dr. Mark Gillespie

Mysteries of Cell Fate Unlocked with New Measurement and Modeling Techniques 

In the cellular process of differentiation, information about the concentrations of an important class of proteins residing in a cell’s nucleus has been lacking, a missing link needed for scientists to fully understand how the process works. ISB researchers have quantified this important class of proteins that play a key role in the formation of red blood cells.

Mysteries of Cell Fate Unlocked with New Measurement and Modeling Techniques 
Mysteries of Cell Fate Unlocked with New Measurement and Modeling Techniques 
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