Dartigalongue, Thibault (2005) Time resolved study of molecular configuration by non linear circular dichroisme. PhD thesis LOB, EP - LOB Laboratoire d'Optique et Biosciences, EP/X p.151.
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Abstract
This work is devoted to the study of photolysis of carbonmonoxy myoglobin (MbCO) followed by time resolved circular dichroism (TRCD). Conformational changes that occur in myoglobin are known to play an important physiological role as a model of the trigger of the a!
llosteric transformation which takes place in hemoglobin. Upon!
ligand dissociation, the heme undergoes an ultrafast doming which propagates along the whole protein through the proximal hisitidine. Experimental measurement of time resolved CD have been carried out in this system. The tricky point was to get rid of the artifact that occurs in such an experiment. A model calculation of CD in myoglobin based on the polarisability theory evidences the key role of the proximal hisitidine. The striking result of this work is a 100 picoseconds dynamics which we assign to a motion of the proximal histidine. A new UV laser source has been built up. The main goal is to follow the first steps of the folding of small polypeptides performing TRCD at 220 nm. Preliminary results are shown.
| Item Type: | PhD Thesis (PhD) |
|---|---|
| Thesis Supervisor: | Hache, François |
| Date: | September 2005 |
| Board of examiners: | Andraud, Chantal and Gustavsson, Thomas and Miller, R. J. Dwayne and Martin, Jean-Louis and Hache, François |
| Ecole Doctorale: | ED 447 ECOLE DOCTORALE DE L'ECOLE POLYTECHNIQUE |
| Discipline: | LOB |
| Collection (Fonds): | EP/X |
| Institution: | EP/X |
| Department: | EP - LOB Laboratoire d'Optique et Biosciences |
| Subjects: | 3. Physics, Optics |
| Uncontrolled Keywords: | Circular dichroism, Myoglobin, Allosteric effect, Protein folding, Dichroïsme circulaire, Myoglobine, Effet allostérique, Repliement des protéines |
| ID Code: | 2115 |
|---|---|
| Deposited By: | Laurence Vidament |
| Deposited On: | 24 January 2007 |
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