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 …

Molecular Insights into the Thermal Stability of mAbs with Variable-Temperature Ion-Mobility Mass Spectrometry

The aggregation of protein-based therapeutics such as monoclonal antibodies (mAbs) can affect the efficacy of the treatment and can even induce effects that are adverse to the patient. Protein engineering is used to shift the mAb away from an aggregation-prone state by increasing the thermodynamic stability of the native fold, which might in turn alter …

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Distinguishing Loss of Structure from Subunit Dissociation for Protein Complexes with Variable Temperature Ion Mobility Mass Spectrometry

Proteins and protein complexes undergo structural changes depending on the surrounding environment, in turn affecting their biological function.  Here, VT-MS is applied to study four multimeric protein complexes and allow for decoupling of their melting temperature (Tm) from the protein complex dissociation temperature (TGPD).   VT-IM-MS is used to investigate structural changes of these proteins at …

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Signature dynamics of intact immunoglobulin G revealed by drift-tube ion-mobility mass spectrometry and molecular modeling

Monoclonal antibodies (mAb) are a rapidly growing group of biopharmaceuticals.  Due to their intrinsic flexibility, intact mAbs provide a challenge with regards to higher order structure characterization.  Intact mAbs and their fragments are explored here using the DT-IM-MS and were found to be far more dynamic in the gas-phase than proteins of comparable size.  This …

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Insights into the Conformations of Three Structurally Diverse Proteins: Cytochrome c, p53, and MDM2, Provided by Variable-Temperature Ion Mobility Mass Spectrometry

Thermally induced conformational transitions of three proteins of increasing intrinsic disorder—cytochrome c, the tumor suppressor protein p53 DNA binding domain (p53 DBD), and the N-terminus of the oncoprotein murine double minute 2 (NT-MDM2)—have been studied by native mass spectrometry and variable-temperature drift time ion mobility mass spectrometry (VT-DT-IM-MS). Ion mobility measurements were carried out at temperatures …

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