About us

Perdita Barran’s Research Group

We develop mass spectrometry based methods and instruments to allow us to look at conformation, conformational change and aggregation. Methods that allow us to preserve non-colvalent protein complexes are also applied to inorganic supramolecular biomimetic systems. We also generate IM-MS data from standard small molecules and proteins that can be used to calibrate TW IM-MS instrumentation.

Our principal areas of research interest are in understanding pre-fibrillar aggregation, intrinsically disordered proteins and how to tame disorder, probing the stability of protein complexes and of model peptide systems.


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Contact us

The Barran Group can be contacted as follows: Professor Perdita E. Barran The Michael Barber Centre for Collaborative Mass Spectrometry Manchester Institute of Biotechnology The University of Manchester 131 Princess Street Manchester M1 7DN, UK t: +44 (0) 161 275 0256 e: perdita.barran@manchester.ac.uk The Manchester Institute of Biotechnology is located in the John Garside Building …

Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy

The early stages of fibril formation are difficult to capture in solution. We use cold‐ion spectroscopy to examine an 11‐residue peptide derived from the protein transthyretin and clusters of this fibre‐forming peptide containing up to five units in the gas phase. For each oligomer, the UV spectra exhibit distinct changes in the electronic environment of …

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Uncoupling conformational states from activity in an allosteric enzyme

ATP-phosphoribosyltransferase (ATP-PRT) is a hexameric enzyme in conformational equilibrium between an open and seemingly active state and a closed and presumably inhibited form. The structure-function relationship of allosteric regulation in this system is still not fully understood. Here, we develop a screening strategy for modulators of ATP-PRT and identify 3-(2-thienyl)-L-alanine (TIH) as an allosteric activator …

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UV Photodissociation Mass Spectrometry Accurately Localize Sites of Backbone Deuteration in Peptides

Hydrogen/deuterium exchange mass spectrometry (HDX-MS) is now a routinely used technique to inform on protein structure, dynamics, and interactions. Localizing the incorporated deuterium content on a single residue basis increases the spatial resolution of this technique enabling detailed structural analysis. Here, we investigate the use of ultraviolet photodissociation (UVPD) at 213 nm to measure deuterium …

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Mobilising ion mobility mass spectrometry for metabolomics

Chromatography-based mass spectrometry approaches (xC-MS) are commonly used in untargeted metabolomics, providing retention time, m/z values and metabolite-specific fragments, all of which are used to identify and validate an unknown analyte. Ion mobility-mass spectrometry (IM-MS) is emerging as an enhancement to classic xC-MS strategies, by offering additional ion separation as well as collision cross section (CCS) determination. …

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