Objective
Vibrational spectroscopy, of which infrared spectroscopy is the most widely applicable, perfectly fills the gap between the structural techniques of X-ray crystallography and NMR, which yield frozen, static structures, and the time- resolved but structurally weak methods of UV/vis and CD spectroscopies. X-ray crystallography and NMR have provided many biomolecular structures while bound substrates and inhibitors have helped in defining the functions. In order to understand the functions of enzymes, redox proteins, DNA-binding proteins and other biological macromolecules in terms of structure, further spectroscopic probes are essential. Raman spectroscopy has fulfilled an important role in time-resolved studies but is applicable only in limited circumstances. IR spectroscopy provides a structural probe with time-resolution and can be used to determine protein secondary structure in equilibrium and on a time resolved basis (folding/unfolding), protein-ligand interaction in enzyme catalysis and inhibition, and the structural changes upon photo reactions and electron transfer reactions. A variety of IR instrumental methods (of which Fourier Transform methods are currently the most widely used) give versatile measurements at very high sensitivity and time resolution, with reasonable effort and cost, and will be applied to these topics in this programme. Isotope- editing coupled with difference methods will allow specific structural features to be highlighted against a dense spectral background, such as a ligand bound to a protein. The interaction of proteins with membranes as well as determination of the mutual perturbing effects of the interaction and the orientation of the protein with respect to the membrane will be measured. Band deconvolution, band fitting, and factor analysis are available for the determination of the secondary structure of proteins, they involve resolution of the components of the overlapping carbonyl bands in the protein spectra and quantitative assignment to specific forms of secondary structure. These methods require further comparison, improvement and evaluation across the range of problems to be addressed in this programme. The theoretical basis of band-fitting procedures and the application of normal mode analysis will be improved. Studies of thermally-induced protein unfolding have shown melting of the various forms of secondary structure as a protein unfolds. No other physical method can provide such direct information concerning this demanding problem, and this method used together with rapid time resolution will be developed to provide detailed data on protein folding processes. The ability to determine the conformation(s) of protein-bound ligands and the changes induced in the protein structure is of great interest, and of immediate application in the pharmaceutical industry. By avoiding the need for frequent complete structural determinations and focusing on the part of the molecule where the interaction occurs, the important structural features will rapidly be highlighted and will speed up the understanding of enzyme mechanism, and applications such as the process of drug design. It is an essential requirement that IR bands observed in biological molecules can be accurately assigned with the help of isotopes, mutants, chemical modifications, and theoretical calculations. A major aim of this programme will be to deliver band assignments which can be applied with confidence. The proposed collaboration will spread knowledge and application of advanced IR technology to actual and new problems in structural biology.
Fields of science (EuroSciVoc)
CORDIS classifies projects with EuroSciVoc, a multilingual taxonomy of fields of science, through a semi-automatic process based on NLP techniques. See: The European Science Vocabulary.
CORDIS classifies projects with EuroSciVoc, a multilingual taxonomy of fields of science, through a semi-automatic process based on NLP techniques. See: The European Science Vocabulary.
- natural sciences earth and related environmental sciences geology mineralogy crystallography
- natural sciences physical sciences optics spectroscopy absorption spectroscopy
- natural sciences biological sciences biochemistry biomolecules proteins protein folding
- natural sciences biological sciences biochemistry biomolecules proteins enzymes
- natural sciences mathematics applied mathematics mathematical model
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Programme(s)
Multi-annual funding programmes that define the EU’s priorities for research and innovation.
Multi-annual funding programmes that define the EU’s priorities for research and innovation.
Topic(s)
Calls for proposals are divided into topics. A topic defines a specific subject or area for which applicants can submit proposals. The description of a topic comprises its specific scope and the expected impact of the funded project.
Calls for proposals are divided into topics. A topic defines a specific subject or area for which applicants can submit proposals. The description of a topic comprises its specific scope and the expected impact of the funded project.
Call for proposal
Procedure for inviting applicants to submit project proposals, with the aim of receiving EU funding.
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Procedure for inviting applicants to submit project proposals, with the aim of receiving EU funding.
Funding Scheme
Funding scheme (or “Type of Action”) inside a programme with common features. It specifies: the scope of what is funded; the reimbursement rate; specific evaluation criteria to qualify for funding; and the use of simplified forms of costs like lump sums.
Funding scheme (or “Type of Action”) inside a programme with common features. It specifies: the scope of what is funded; the reimbursement rate; specific evaluation criteria to qualify for funding; and the use of simplified forms of costs like lump sums.
Coordinator
91056 Erlangen
Germany
The total costs incurred by this organisation to participate in the project, including direct and indirect costs. This amount is a subset of the overall project budget.