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Theoretical study of the hemoglobin co-operative oxygen binding mechanism byquantum mechanical and molecular dynamics calculations

Objective



Research objectives and content
Hemoglobin is one of the most important proteins in the vertebrate organisms playing the fundamental rtle of oxygen carrier. A better knowledge of its structural characteristics at the atomic level for the oxygen binding is essential for the synthesise of artificial blood, on of the central goal of pharmaceutical industry. This research project aims at the full characterisation through theoretical methods of the binding mechanism. The novelty of this project with respect to previous studies will come from the application of novel theoretical hybrid methods that had not been considered before (IMMON) to state of-the-act molecular dynamics calculations. IMMOM, though its combination of quantum mechanics and molecular mechanics ought to improve substancially our knowledge of the rtle played by the oxygen bindingenvironment. This approach will hopefully provide the first accurate description of the atomic movements involved in the fination of each of the four oxygen molecules bound by each protein sub-unit.
Training content (objective, benefit and expected impact)
This project will offer me the possibility of learning the major theoretical methods and a new one used in chemistry and biochemistry, and to apply them to systems never studied at the atomic level in the bioinorganic.
Links with industry / industrial relevance (22)
The results of these studies should have an important impact on pharmaceutical industry.

Funding Scheme

RGI - Research grants (individual fellowships)

Coordinator

AUTONOMOUS UNIVERSITY OF BARCELONA
Address
Campus Universitario, Edificio C
08193 Bellaterra
Spain

Participants (1)

Not available
France