CIDNP_OF_BM · CIDNP study of photochemically generated short lived radical intermediates of biologically important molecules
FP6 — Marie Curie Actions (Human Resources and Mobility)
- Duration
- 2006-07-01 → 2008-06-30
- EU contribution
- €212,388
- Participants
- 1
- Scheme
- IIF
Lines connect the coordinator with its partners. CORDIS does not always give exact coordinates for projects before 2014. These points are placed at city or country level.
Results in brief
Final Activity Report Summary - CIDNP_of_BM (CIDNP study of photochemically generated short lived radical intermediates of biologically important molecules)
Experimental and theoretical techniques based on magnetic resonance were developed and applied to obtain data on the structure and reactivity of radical states of structural building blocks of proteins and nucleic acids, namely amino acids and nucleotides, which were crucial for understanding the mechanisms of numerous biochemical processes. The results of these studies were used to probe the structure and dynamics of native and unfolded proteins with promising subsequent applications in numerous branches of biochemistry. The modelling of non-enzymatic deoxyribonucleic acid (DNA) repair by electron transfer from amino acids to oxidised purine nucleotide guanosine monophosphate was studied as a prototype of fast chemical repair of radiation-induced DNA damages. We showed that chemically-induced dynamic nuclear polarisation (CIDNP), in particular its field dependence and time-resolved version, could be applied as routine techniques for determining the magnetic resonance parameters of elusive radical species that could not be detected by electron paramagnetic resonance (EPR) spectroscopy. In addition, the CIDNP technique was used as tool for protein studies, providing a strong signal enhancement compared to conventional nuclear magnetic resonance (NMR) and giving new information on residue accessibility and mobility in proteins in different states, thus allowing for obtaining quantitative data about correlation times of intramolecular motions of residues on the nanosecond timescale.
Data: CORDIS, © European Union
Project objective
The project is aimed at the application and further development of a novel non-destructive NMR method of high sensitivity, chemical selectivity, and high spectral resolution. The method is based on chemically induced dynamic nuclear polarization (CIDNP) for studying the structure and dynamic processes of biological macromolecules at physiological conditions.We propose to utilize the nuclear spin polarization that is formed in the reversible light-induced radical reactions of dye markers with proteins and nucleic acids and their structural subunits (amino acids, peptides, nucleotides, oligonucleotides) in aqueous solution and to expand the application of the method to similar processes in the solid state.The research methodology includes application of three types of CIDNP experiments:- with time-resolution,- with magnetic field variation by field-cycling, and- with resonant pumping of electronic spin transitions for NMR detection of EPR spectra of spin correlated radicals pairs in combination with field-cycling.The project has an interdisciplinary character and includes biological, photochemical, and physical approaches.The research activities are associated with the following:- The study of photochemical reactions involving proteins and protein-related molecules will create a reliable basis for studying proteins using the CIDNP technique, and will contribute to the knowledge of photochemistry of biopolymers.- The investigation of native, partially folded and denatured states of proteins, as well as the study of the processes of denaturation and folding will be compared with the theoretical modeling of protein dynamics.- Development and application of MAS-NMR detection of time evolution and field dependence of nuclear polarization in proteins in solid state.
Original text from CORDIS.
Participants
- FREIE UNIVERSITAET BERLIN (FREE UNIVERSITY OF BERLIN, DEPARTMENT OF PHYSICS) · BERLINCoordinatorCity levelGermany
Links
Data: CORDIS, © European Union