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Dr Peter Adams
Prof Stephen Muench
No more applications being accepted
Competition Funded PhD Project (European/UK Students Only)
About the Project
Understanding the biophysics of photosynthesis could provide clues to developing the next generation of crops. Light-Harvesting Complex II (LHCII) is the main protein in plants that absorbs solar photons and channels energy to where it is needed. LHCII is estimated to be the most abundant membrane protein on Earth and is essential for efficient photosynthesis, yet, its crucial role in “photoprotection” has an unknown mechanism. This project will use cutting-edge biochemical and biophysical techniques and our world-class microscopy facilities to study how LHCII can switch between different states. Project aims: (1) to determine a high-resolution structure of the LHCII in the “light-harvesting” vs “protected” state, (2) to quantify what triggers photoprotection in LHCII by analyzing “model membranes”, (3) to correlate changes in molecular structure with changes in function towards a definitive mechanism. To do this, LHCII will be biochemically purified and characterized with state-of-the-art fluorescence techniques in parallel with single-particle cryo electron microscopy. You will use LHCII either isolated in detergent suspension or incorporated within nanoscale lipid bilayers to test the effect of lipids. This will provide insight into the biophysical basis of photosynthetic processes crucial for life on Earth but poorly understood.
Funding Notes
White Rose BBSRC Doctoral Training Partnership in Mechanistic Biology
4 year fully-funded programme of integrated research and skills training, starting Oct 2020:
• Research Council Stipend
• UK/EU Tuition Fees
• Conference and research funding
Requirements:
At least a 2:1 honours degree or equivalent. We welcome students with backgrounds in biological, chemical or physical sciences, or mathematical backgrounds with an interest in biological questions.
EU candidates require 3 years of UK residency to receive full studentship
Not all projects will be funded; the DTP will appoint a limited number of candidates via a competitive process.
https://phd.leeds.ac.uk/funding/81-white-rose-bbsrc-doctoral-training-partnership-in-mechanistic-biology
4 year fully-funded programme of integrated research and skills training, starting Oct 2020:
• Research Council Stipend
• UK/EU Tuition Fees
• Conference and research funding
Requirements:
At least a 2:1 honours degree or equivalent. We welcome students with backgrounds in biological, chemical or physical sciences, or mathematical backgrounds with an interest in biological questions.
EU candidates require 3 years of UK residency to receive full studentship
Not all projects will be funded; the DTP will appoint a limited number of candidates via a competitive process.
https://phd.leeds.ac.uk/funding/81-white-rose-bbsrc-doctoral-training-partnership-in-mechanistic-biology
References
1. Hancock, AM; Meredith, SA; Connell, SDA; Jeuken, LJC; Adams, PG (2019) Proteoliposomes as energy transferring nanomaterials: enhancing the spectral range of light-harvesting proteins using lipid-linked chromophores. Nanoscale 11, 16284-16292.
2. Adams PG; Vasilev C; Neil Hunter C; Johnson MP (2018) Correlated fluorescence quenching and topographic mapping of Light-Harvesting Complex II within surface-assembled aggregates and lipid bilayers. BBA Bioenergetics 1859, 1075-1085.
3. Kontziampasis, D, Klebl, DP, Iadanza, MG, Scarff, CA, Kopf, F, Sobott, F, Monteiro, CF, Trebbin, M, Muench SP. & White HD. A cryo-EM grid preparation device for time-resolved structural studies. (2019) IUCrJ 6, DOI: 10.1107/S2052252519011345.
4. Agip AA, Blaza JN, Bridges HR, Viscomi C, Rawson S, Muench SP, Hirst J. (2018) Cryo-EM structures of complex I from mouse heart mitochondria in two biochemically defined states. Nat Struct Mol Biol. 7, 548-556.
5. Rawson S, Bisson C, Hurdiss DL, Fazal A, McPhillie MJ, Sedelnikova SE, Baker PJ, Rice DW, Muench SP. (2018) Elucidating the structural basis for differing enzyme inhibitor potency by cryo-EM. Proc Natl Acad Sci U S A. 115, 1795-1800.
2. Adams PG; Vasilev C; Neil Hunter C; Johnson MP (2018) Correlated fluorescence quenching and topographic mapping of Light-Harvesting Complex II within surface-assembled aggregates and lipid bilayers. BBA Bioenergetics 1859, 1075-1085.
3. Kontziampasis, D, Klebl, DP, Iadanza, MG, Scarff, CA, Kopf, F, Sobott, F, Monteiro, CF, Trebbin, M, Muench SP. & White HD. A cryo-EM grid preparation device for time-resolved structural studies. (2019) IUCrJ 6, DOI: 10.1107/S2052252519011345.
4. Agip AA, Blaza JN, Bridges HR, Viscomi C, Rawson S, Muench SP, Hirst J. (2018) Cryo-EM structures of complex I from mouse heart mitochondria in two biochemically defined states. Nat Struct Mol Biol. 7, 548-556.
5. Rawson S, Bisson C, Hurdiss DL, Fazal A, McPhillie MJ, Sedelnikova SE, Baker PJ, Rice DW, Muench SP. (2018) Elucidating the structural basis for differing enzyme inhibitor potency by cryo-EM. Proc Natl Acad Sci U S A. 115, 1795-1800.
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Career overview
Dr. Peter Adams is an Associate Professor in the School of Physics and Astronomy at the University of Leeds, where he has been a part of the Molecular and Nanoscale Physics research group since 2015. He completed his PhD in Biochemistry and Microbiology at the University of Sheffield from 2007 to 2011, following a BSc in the same field from 2004 to 2007. Prior to his current position, Dr. Adams worked as a Postdoctoral Research Scholar at Los Alamos National Laboratory in the USA from 2012 to 2014. His academic journey reflects a strong foundation in biochemistry and microbiology, which he has built upon through his research and teaching roles.
Research interests
Dr. Adams'' research investigates membrane protein and lipid assembly, focusing on specialized “light-harvesting” membranes involved in photosynthesis. His work aims to understand, mimic, and control the organization of membranes inspired by the light-harvesting membranes found within plants (chloroplasts) and photosynthetic bacteria. He employs a multi-disciplinary approach that combines surface chemistry, nano/micro fabrication, protein biochemistry, spectroscopy, and various microscopy techniques. 1. Biophysics of natural “light-harvesting” membranes of photosynthesis: A major goal is to understand the role of plant Light-Harvesting Complex II (LHCII) in photoprotection. Dr. Adams studies the molecular mechanism of the photoprotective process known as “nonphotochemical quenching” and has a longstanding interest in the light-harvesting membranes from purple bacteria and the “chlorosome” antennae of green bacteria. 2. Model biomembranes, artificial photosynthesis, and nanotechnology: He aims to develop novel nanocomposites for energy transfer using purified light-harvesting proteins, natural and synthetic lipids, quantum dots, and polymers as building blocks to create model protein/lipid systems. His research explores lipid bilayers as platforms to study lipid biophysics and protein function, allowing for biologically relevant characterisation through advanced microscopy. 3. Advanced microscopy and spectroscopy of various biophysical samples: Dr. Adams is interested in using Atomic Force Microscopy (AFM) to investigate natural and synthetic membranes and protein arrangements. He also employs time-resolved fluorescence spectroscopy and fluorescence microscopy (TCSPC and FLIM) to explore the photophysical properties of biological and nanophotonic materials.
Biophysics
Photosynthesis
Light-Harvesting Proteins
Lipid Membranes
Atomic Force Microscopy
Fluorescence Spectroscopy
Fluorescence Lifetime Imaging Microscopy
Nanomaterials
Membrane Protein Assembly
Lipid Assembly
Photoprotection
Light-Harvesting Complex II
Nonphotochemical Quenching
Model Biomembranes
Artificial Photosynthesis
Nanocomposites
Energy Transfer
Lipid Bilayers
Advanced Microscopy
Time-Resolved Fluorescence Spectroscopy
Nanophotonic Materials
Career overview
Dr Stephen Muench studied for an undergraduate degree in Biochemistry and Microbiology at the University of Sheffield in 1997, during which time he undertook an undergraduate research project in X-ray crystallography, fostering his strong interest in structural biology. He continued at Sheffield for his PhD studies, focusing on the development of new anti-malarial and toxoplasmosis compounds through X-ray crystallography. After a brief postdoctoral position in Sheffield studying the role of the GTPase EngA, he moved to Leeds in 2005 to learn electron microscopy (EM). During this time, he developed a keen interest in EM and its application for studying large membrane protein complexes, as well as new methodologies such as time-resolved cryoEM. Following the award of an MRC career development fellowship in 2010, he established his own research group with a strong interest in combining different techniques to study the structure and function of a wide range of protein targets. Dr Muench is currently an Associate Professor in Membrane Biology at the University of Leeds, where his group has worked on various systems and technologies, including the development of new small molecules, membrane protein scaffolds, biosensors, and time-resolved approaches. Major contributions to the field include the use of EM to drive inhibitor design for membrane proteins, development of time-resolved methodologies for cryoEM, and advancements in understanding sample preparation within single particle cryoEM.
Research interests
Dr Muench''s research focuses on structural biology, particularly the dynamics and conformational variability of large protein complexes. His work employs a combination of techniques, including X-ray crystallography and electron microscopy (EM), with an emphasis on time-resolved applications. He is involved in developing new approaches for sample preparation and time-resolved cryoEM studies, aiming to enhance the understanding of the structure/function relationship of medically important targets. Dr Muench''s research includes the development of time-resolved cryoEM methodologies, which allow for the trapping of dynamic protein states at various points in their movement. This involves collaboration with experts in engineering, mass spectrometry, and chemistry to create systems that can capture protein behaviours on the second, millisecond, and microsecond timescales. His group has also investigated the stability of samples for single particle cryoEM, revealing the time-dependent nature of sample stability and degradation. In addition, Dr Muench is focused on improving the study of membrane proteins, which are crucial for drug targeting but are less understood than soluble proteins. His research explores the use of styrene maleic acid (SMA) and related copolymers to extract and stabilise membrane proteins in a more native lipid environment. This work has led to significant advancements, including the first negative stain and sub-nanometre single particle cryoEM structure of an SMA-extracted membrane protein. Dr Muench''s interests also extend to structure-based drug design, where he aims to develop new small molecule inhibitors and understand disease-causing mutations across various diseases. His collaborative projects span multiple areas of biology, involving national and international partners, and include studies on TRPC channels, receptor tyrosine kinases, ABC transporters, and myosin, among others.
Membrane Biology
Structural Biology
Electron Microscopy
Membrane Proteins
Structure Based Drug Design
Time Resolved Electron Microscopy
Sample Preparation
X-Ray Crystallography
Protein Dynamics
CryoEM
Small Molecule Inhibitors
Protein Expression
Styrene Maleic Acid
Native Lipids
Drug Targeting
Biochemical Analysis
Protein Complexes
Biosensors
Method Development
Conformational Variability
Therapeutic Targets.
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