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Prof Sheena Radford
Prof Neil Ranson
No more applications being accepted
Competition Funded PhD Project (European/UK Students Only)
About the Project
Amyloidosis is a pathological condition associated with the aggregation of proteins into fibrils, and is the underlying pathology of diseases such as Alzheimer’s and Parkinson’s diseases. Despite the increasing importance of amyloid diseases in today’s ageing population, therapies remain remote.
In this project we will use state of the art imaging technologies to gain fundamental insights into the structure of amyloid fibrils, how they form and how they interact with cellular components. Specifically, using powerful Titan Krios electron microscopes recently installed in the Astbury Centre for Structural Molecular Biology at Leeds we will use cryo-EM to determine the structure of amyloid fibrils formed from the protein 2-microglobulin and natural variants which cause enhanced amyloid disease. Using biochemical and biophysical assays, combined with cryo-electron microscopy, we will also determine the structure of amyloid assembly intermediates and examine how they bind essential cellular components including molecular chaperones. Finally, we will use cell biology, super resolution imaging, cryo-electron tomography and cryo X-ray tomography to examine fibril formation within living cells.
Overall, therefore, the aim is to provide new insights into amyloid fibril structure and fibril-induced cellular interactions and amyloid-induced cytotoxicity by exploiting modern cryo-EM to the full.
More details about research in our research groups can be found at:
http://bmbsgi10.leeds.ac.uk
http://www.astbury.leeds.ac.uk.
Please contact [Email Address Removed] for more information.
In this project we will use state of the art imaging technologies to gain fundamental insights into the structure of amyloid fibrils, how they form and how they interact with cellular components. Specifically, using powerful Titan Krios electron microscopes recently installed in the Astbury Centre for Structural Molecular Biology at Leeds we will use cryo-EM to determine the structure of amyloid fibrils formed from the protein 2-microglobulin and natural variants which cause enhanced amyloid disease. Using biochemical and biophysical assays, combined with cryo-electron microscopy, we will also determine the structure of amyloid assembly intermediates and examine how they bind essential cellular components including molecular chaperones. Finally, we will use cell biology, super resolution imaging, cryo-electron tomography and cryo X-ray tomography to examine fibril formation within living cells.
Overall, therefore, the aim is to provide new insights into amyloid fibril structure and fibril-induced cellular interactions and amyloid-induced cytotoxicity by exploiting modern cryo-EM to the full.
More details about research in our research groups can be found at:
http://bmbsgi10.leeds.ac.uk
http://www.astbury.leeds.ac.uk.
Please contact [Email Address Removed] for more information.
Funding Notes
BBSRC White Rose Mechanistic Biology DTP 4 year studentship.
Studentships covers UK/EU fees and stipend (c.£14,553) for 4 years to start in Oct 2018. Applicants should have/be expecting at least a 2.1 Hons. degree in a relevant subject. EU candidates require 3 years of UK residency in order to receive full studentship.
Not all projects advertised will be funded; the DTP will appoint a limited number of candidates via a competitive process and the projects selected by the successful candidates will be funded.
There are 2 stages to the application process. Please see our website for more information: http://www.fbs.leeds.ac.uk/postgraduate/phdopportunities.php
Studentships covers UK/EU fees and stipend (c.£14,553) for 4 years to start in Oct 2018. Applicants should have/be expecting at least a 2.1 Hons. degree in a relevant subject. EU candidates require 3 years of UK residency in order to receive full studentship.
Not all projects advertised will be funded; the DTP will appoint a limited number of candidates via a competitive process and the projects selected by the successful candidates will be funded.
There are 2 stages to the application process. Please see our website for more information: http://www.fbs.leeds.ac.uk/postgraduate/phdopportunities.php
References
We have published several exciting papers on this topic recently. A full list of publications can be found on the web site http://www.astbury.leeds.ac.uk and then look up Radford.
Further details about the Radford group can be found at http://www.astbury.leeds.ac.uk/bmbsgi10
Further details about the Radford group can be found at http://www.astbury.leeds.ac.uk/bmbsgi10
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Career overview
Professor Sheena Radford joined the University of Leeds in 1995 as a Lecturer in the School of Biochemistry and Molecular Biology, progressing to Reader in 1998 and Professor in 2000. In 2009, she became the Deputy Director of the Astbury Centre for Structural Molecular Biology, and served as its Director from 2012 to 2021. She was appointed Astbury Professor of Biophysics in 2014 and became a Royal Society Research Professor in 2021. Professor Radford graduated with a BSc in Biochemistry from the University of Birmingham and completed her PhD in Biochemistry at the University of Cambridge under the supervision of Professor R.N. Perham, FRS. She has held various postdoctoral positions and a Royal Society University Research Fellowship at the Oxford Centre for Molecular Sciences. Throughout her career, Professor Radford has supervised around 25 PhD students and postdoctoral researchers in her laboratory, with over 160 individuals successfully progressing from her lab into various careers in academic research, industry, and technical editing. She has published more than 360 peer-reviewed papers and book chapters and has delivered over 475 invited lectures at national and international conferences across numerous countries. In the last five years, she has served on five major research funding panels and 20 Scientific Advisory Boards for prestigious institutions and companies. Additionally, she has been involved with editorial boards for several journals and currently serves as an Associate Editor for the Journal of Molecular Biology. She is also a Trustee and Council member of the Dementia Research Institute, UK, and the Regional Champion for the Academy of Medical Sciences. Professor Radford has received multiple awards, including the Biochemical Society Colworth Medal in 1996, the Royal Society of Chemistry AstraZeneca Prize in 2005, the Hites Award from the American Society for Mass Spectrometry in 2009, the Protein Society Carl Branden Award in 2013, and the Rita and John Cornforth Award of the Royal Society of Chemistry in 2015. She was elected a member of EMBO in 2007, a member of Academia Europaea in 2020, and has been recognised as a Fellow of the Academy of Medical Sciences (2010), the Royal Society (2014), and the Royal Society of Biology (2021). She was made an honorary member of the British Biophysical Society in 2014 and a Fellow of the Biophysical Society in 2018. In 2022, she received an honorary doctorate from the University of Liège, and in 2024, she became an International Member of the National Academy of Sciences (USA).
Research interests
Professor Radford''s research focuses on fundamental structural molecular biology, specifically the measurement of the conformational dynamics of proteins and the elucidation of the role that these motions play in protein folding and misfolding of both water-soluble and membrane proteins. Their research employs a wide range of biophysical methods, combining techniques from protein chemistry, molecular biology, chemical biology, and structural biology. Over the last 35 years, they have concentrated on delineating the mechanisms by which proteins fold or misfold, how dynamic excursions enable proteins to self-associate into amyloid fibrils—which are complex macromolecular assemblies associated with some of the deadliest human diseases—and how proteins fold into the bacterial outer membranes of Gram-negative organisms. Current major projects include: Mechanism(s) of protein misfolding and assembly into amyloid, Outer Membrane Protein (OMP) folding – The role of chaperones & BAM, Stabilising proteins of therapeutic interest against aggregation, Method development (MS, NMR, single molecule, biophysical methods).
Protein Folding
Protein Misfolding
Protein Aggregation
Amyloid
Membrane Protein Folding
Biopharmaceuticals
Structural Molecular Biology
Biophysical Methods
Protein Chemistry
Chemical Biology
Cell Biology
Conformational Dynamics
Mechanisms of Protein Folding
Therapeutic Proteins
Dynamic Excursions
Self-Association
Gram-Negative Bacteria
Chaperones
Method Development
Mass Spectrometry
NMR
Single Molecule Techniques.
Career overview
Professor Neil Ranson studied for a Biochemistry degree and subsequently completed a PhD in Mechanistic Enzymology at the University of Bristol under the supervision of Professor Tony Clarke. His doctoral research focused on understanding how the molecular chaperones GroEL and GroES assist in the folding of proteins within the crowded cellular environment. He then transitioned into structural biology, working with Professor Helen Saibil at Birkbeck College, London. Professor Ranson joined the University of Leeds as a University Research Fellow in 2002 and has progressed through roles as a Lecturer and Associate Professor to his current position as Professor of Structural Molecular Biology. He serves as the Director of The Astbury Centre for Structural Molecular Biology and the Director of Electron Microscopy at the Astbury Biostructure Laboratory.
Research interests
Professor Ranson''s research focuses on the structure of macromolecules such as proteins and nucleic acids, as well as the dynamic, heterogeneous complexes they form that drive biological function. A major area of interest is structural virology, where the lab investigates various aspects of virus structure using cryo-electron microscopy, including virus assembly, uncoating, and virus-receptor interactions. The lab is currently working on a diverse range of viral pathogens that are significant for food security and human health. Additionally, Professor Ranson''s lab maintains a strong interest in protein folding studies, exploring how proteins fold into membranes and the mechanisms of protein misfolding that lead to amyloidoses.
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