EPR spectroscopy of protein microcrystals oriented in a liquid crystalline polymer medium.
Correlation of the g-tensor of a paramagnetic active center of a protein with its structure provides a unique experimental information on the electronic structure of the metal site. To address this problem, we made solid films containing metalloprotein (Desulfovibrio gigas cytochrome c(3)) microcrystals. The microcrystals in a liquid crystalline polymer medium (water/hydroxypropylcellulose) were partially aligned by a shear flow. A strong orientation effect of the metalloprotein was observed by EPR spectroscopy and polarizing optical microscopy. The EPR spectra of partially oriented samples were simulated, allowing for molecular orientation distribution function determination. The observed effect results in enhanced sensitivity and resolution of the EPR spectra and provides a new approach towards the correlation of spectroscopic data, obtained by EPR or some other technique, with the three-dimensional structure of a protein or a model compound.
Caldeira
Jorge
J
Requimte/Centro de Química Fina e Biotecnologia, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal. fjc@dq.fct.unl.pt
Figueirinhas
João Luis
JL
Santos
Celina
C
Godinho
Maria Helena
MH
D002482:Cellulose / Q000031:analogs & derivatives*; D003460:Crystallization; D003574:Cytochrome c Group / Q000737:chemistry*; D003901:Desulfovibrio / Q000201:enzymology*; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D011108:Polymers; D012256:Riboflavin / Q000737:chemistry; D012996:Solutions
D003574:Cytochrome c Group; D011108:Polymers; D012996:Solutions; D002482:Cellulose; C017165:cytochrome c(3); C008079:hydroxypropylcellulose; D012256:Riboflavin