CIDNP study of photochemically generated short lived radical intermediates of biologically important molecules

Projektinformationen

CIDNP_OF_BM

ID Finanzhilfevereinbarung: 22008

Projekt abgeschlossen

Startdatum 1 Juli 2006

Enddatum 30 Juni 2008

Finanziert unter

• Human resources and Mobility in the specific programme for research, technological development and demonstration "Structuring the European Research Area" under the Sixth Framework Programme 2002-2006

Gesamtkosten € 0,00

EU-Beitrag € 212 388,00

Koordiniert durch

FREIE UNIVERSITAET BERLIN (FREE UNIVERSITY OF BERLIN, DEPARTMENT OF PHYSICS)
Germany

Ziel

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.

Wissenschaftliches Gebiet

• natural sciences › biological sciences › biochemistry › biomolecules › nucleic acids
• natural sciences › chemical sciences › physical chemistry › photochemistry
• natural sciences › biological sciences › biochemistry › biomolecules › proteins
• natural sciences › biological sciences › genetics › nucleotides
• natural sciences › chemical sciences › organic chemistry › amines

Schlüsselbegriffe

• MAS -NMR
• NMR
• chemically induced dynamic nuclear polarization
• electron spin polarization
• photoinduced electron transfer
• spin correlated radical pair
• structure and dynamics of biomolecules

Programm/Programme

• FP6-MOBILITY - Human resources and Mobility in the specific programme for research, technological development and demonstration "Structuring the European Research Area" under the Sixth Framework Programme 2002-2006

Thema/Themen

• MOBILITY-2.3 - Marie Curie Incoming International Fellowships (IIF)

Aufforderung zur Vorschlagseinreichung

FP6-2004-MOBILITY-7
Andere Projekte für diesen Aufruf anzeigen

Finanzierungsplan

IIF - Marie Curie actions-Incoming International Fellowships

Koordinator

FREIE UNIVERSITAET BERLIN (FREE UNIVERSITY OF BERLIN, DEPARTMENT OF PHYSICS)

• EU-Beitrag: Keine Daten
• Adresse: Kaiserswerther Strasse 16-18 ; BERLIN ; Deutschland
• Gesamtkosten: Keine Daten