
University of Leeds
ISNI: 0000000419368403
FundRef: 501100000777 , 501100003466 , 501100004294
RRID: RRID:SCR_004863 , RRID:nlx_34628
ISNI: 0000000419368403
FundRef: 501100000777 , 501100003466 , 501100004294
RRID: RRID:SCR_004863 , RRID:nlx_34628
University of Leeds
Funder
4,316 Projects, page 1 of 864
assignment_turned_in Project2004 - 2007Partners:University of LeedsUniversity of LeedsFunder: UK Research and Innovation Project Code: G84/6495Funder Contribution: 181,580 GBPAbstracts are not currently available in GtR for all funded research. This is normally because the abstract was not required at the time of proposal submission, but may be because it included sensitive information such as personal details.
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For further information contact us at helpdesk@openaire.euassignment_turned_in Project2010 - 2015Partners:University of LeedsUniversity of LeedsFunder: UK Research and Innovation Project Code: G1000567Funder Contribution: 705,357 GBPThe vacuolar ATPase (V-ATPase) is a complex multi-component protein found in virtually all living cells. It is a miniature mechanical rotary motor, only thirty millionths of a millimetre long but capable of pushing protons into or out of specialised compartments in the cell, regulating acidity. The V-ATPase is a 3-stroke motor that uses ATP as a fuel to rotate a central axle, which is linked to a 10-stroke acid pump plugged into the cell membrane. A molecular gearbox links the two motors allowing it to push protons against different gradients. However, the way in which the motors work and are controlled by the cell are still unclear. This project aims to generate a high resolution structure, through electron microscopy and X-ray crystallography, revealing the composition and mechanism of this motor and its gearbox. Understanding the structure and mechanism of this motor will provide important information which can be used to develop new drugs, important because of the role the protein plays in a number of diseases including osteoporosis, kidney disease and cancer. By understanding the structure, mechanism and regulation of the protein we may be able to develop novel ways of switching it off with drugs in diseased tissue.
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For further information contact us at helpdesk@openaire.euassignment_turned_in Project2017 - 2022Partners:University of LeedsUniversity of LeedsFunder: UK Research and Innovation Project Code: 2116851Soap bars (based on sodium salts of fatty acids) and syndet bars (using added sodium salts of isethionate esters) suffer from the presence of grit like spherical particles. These hard particles cause extensive manufacturing problems (such as difficulty in melting the pre-bar blends) and are disliked by the consumer. Grit is formed in the initial crystallisation/precipitation of the soap ingredient and various ingredients are subsequently blended and melted before pressing out into bars. The presence of grit affects all the downstream processing stages - these hard lumps cause equipment erosion and slow down the melting process, block filters and so on. Grit also abrades skin when washing and has an unpleasant feel. This has assisted the uptake of liquid soaps and body washes in the West. However, the use of liquid soaps has increased the need for packaging and the emission of more greenhouse gases due to transporting what is effectively water. Innospec is the only Western major player doing research in this area and cannot make the next step in utilising new improved ingredients which will result in a change in consumer preference. A successful outcome would result in Innospec (with its research base in the UK) becoming the largest European supplier of key ingredients for a rejuvenated soap bar market. A multi-disciplinary approach utilising the CDT in Complex Particulate Products and Processes is required to fully characterise these grit particles for the first time and to identify routes for their prevention or elimination. This project builds on the research of Cohort 1 CDT student Mohammed Jeraal. Reference: Process-Focused Synthesis, Crystallization, and Physicochemical Characterization of Sodium Lauroyl Isethionate - https://pubs.acs.org/doi/abs/10.1021/acssuschemeng.7b04237 Aims: To define the crystallisation processing boundaries that form grit in soap bars and to develop counter measures to reduce or eliminate grit. Objectives: Develop measurement/analytical methods to determine the effect of the current manufacturing process that leads to the formation of grit. Examine the dynamics of the melt crystallization in-situ as a function of rheological behaviour and crystallization supersaturation. Study the influence of the ingredient composition and impurities on the crystallisation process specifically addressing how this impacts upon the resultant melt viscosity and particle aggregation in solution. Understand and characterise ingredient and product crystallisation kinetics and its inter-relationship with particle morphology (crystal form) and develop a process model for the manufacturing process. Develop an understanding of what factors affect the crystal form, grit formation and its elimination - this will cover assessing the current synthesis conditions, the effect of impurities, chemical additives and the potential to change the fundamental chemistry by the use of other ingredients.
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For further information contact us at helpdesk@openaire.euassignment_turned_in Project2008 - 2013Partners:University of LeedsUniversity of LeedsFunder: European Commission Project Code: 228035All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=corda_______::f89d0abff6a0035e51634d20a76dc572&type=result"></script>'); --> </script>
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For further information contact us at helpdesk@openaire.euOpen Access Mandate for Publications and Research data assignment_turned_in Project2018 - 2020Partners:University of LeedsUniversity of LeedsFunder: European Commission Project Code: 795471Overall Budget: 195,455 EURFunder Contribution: 195,455 EURThis project is concerned with integrable many-body systems of Calogero-Ruijsenaars type. It aims at finding new models, related algebraic structures, and connections to various field theories. The most important outcomes to be expected are the following: 1. Discovery of quantum and classical Lax pairs for hyperbolic, trigonometric, and elliptic relativistic models containing multiple couplings. 2. Solution of the classical and quantum dynamics of new compactified trigonometric relativistic systems. 3. Finding new and extending already existing links to quiver gauge theory and topological quantum field theory. Integrable models of Calogero-Ruijsenaars type describe the pairwise interaction of equal-mass particles moving on a line or circle. The strength of particle interaction is regulated by a (real) number, the coupling parameter. Setting this parameter to zero means no interaction, i.e. free particles, while non-zero parameter values result in a complicated motion. This is due to the non-linear pair potential, of which we distinguish four types, named rational, hyperbolic, trigonometric, and elliptic. The particles can be thought of as either non-relativistic bodies obeying the laws of Newtonian mechanics or relativistic point masses with an upper speed limit (given by the speed of light). Integrable quantum mechanical versions also exist. In addition, Calogero-Ruijsenaars type systems have several generalisations preserving integrability, such as models in external fields (involving multiple couplings) or particles with spin (internal degrees of freedom). This profusion of variants enhances the importance of these systems. In fact, Calogero-Ruijsenaars type models are intimately related to various integrable systems of seemingly different character. These include soliton equations (e.g. Korteweg-de Vries equation and sine-Gordon equation), lattice models (e.g. Toda model), solvable spin and vertex models (e.g. Heisenberg XYZ model and 8-vertex model).
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