Biochemistry

Quantifying protein interactions in real time via dipole relaxation frequency

Royal Holloway, University of London

Not stated

Location
Egham, United Kingdom, United Kingdom
Funding
Self-Funded PhD Students Only
Application deadline
Year-round applications

About the project

About the Project Proteins are large, complex molecules with an uneven distribution of polarizable and ionizable amino acids, and they often possess a dipole moment. If an external electric field is applied, the protein dipole will attempt to physically rotate to align itself with the electric field lines. Each protein or protein complex possesses a characteristic relaxation time needed to reach a new equilibrium when the field changes, or the time it takes for the molecule to return to a random orientation after the field is removed. The relaxation frequency, which is inversely proportional to this time, characterizes the specific rate at which a protein molecule rotates to align itself with an external alternating current (AC) electric field. Relaxation frequency is governed by the Stokes-Einstein-Debye relationship and depends on the hydrodynamic volume of the protein, and therefore the protein's size and shape, the viscosity of the solvent, and the temperature. Therefore, measuring relaxation frequency should allow for the detection of molecular interactions, such as antibody-antigen binding, or structural changes, such as protein binding kinetics, unfolding, or aggregation, in real-time. The aim of this PhD research project is to devise and test an AC/DC test platform for detecting and quantifying protein-protein binding kinetics and to apply the newly developed approach to characterizing antibody-antigen and protein-small molecule interactions. The research will be conducted in the Department of Biological Sciences, Royal Holloway, University of London. Eligibility: Applicants should have at least an Upper Second (2:1) undergraduate degree (or equivalent) in Chemistry, Biochemistry, Biomedical Sciences, Biological Sciences, or another related discipline, or a Master’s degree (or international equivalent) in a relevant science or engineering field. They should also have an interest in molecular engineering, protein-protein or protein-DNA interactions, assay development, or a related area of bioanalytical sciences. Applicants must meet the University’s English language requirements. Before you apply: Prior to submitting their online application, the applicants are encouraged to contact the supervisor directly. Please include a full CV in your email, specifying details of subjects studied and any research projects undertaken, outline your research interests and preferences, and specify the preferred start date. How to apply The online application can be submitted any time. Detailed application information can be found here: https://www.royalholloway.ac.uk/studying-here/applying/research-degrees/

Research areas

BiochemistryBioengineeringBiophysicsBiotechnologyMolecularBiologyBiologicalSciencesPhysicalChemistryQuantifyingproteininteractionsinrealtimeviadipolerelaxationfrequency