tailieunhanh - Báo cáo khoa học: Protein stabilization by compatible solutes Effect of diglycerol phosphate on the dynamics of Desulfovibrio gigas rubredoxin studied by NMR

Heteronuclear NMR relaxation measurements and hydro-gen exchange data have been used to characterize protein dynamics in the presence or absence of stabilizing solutes from hyperthermophiles. Rubredoxin from Desulfovibrio gigaswas selected as a model protein and the effect of diglycerol phosphate on its dynamic behaviour was studied. The presence of 100 mMdiglycerol phosphate induces a fourfold increase in the half-life for thermal denaturation ofD. | Eur. J. Biochem. 270 4606-4614 2003 FEBS 2003 doi Protein stabilization by compatible solutes Effect of diglycerol phosphate on the dynamics of Desulfovibrio gigas rubredoxin studied by NMR Pedro Lamosa1 David L. Turner1 2 Rita Ventura1 Christopher Maycock1 and Helena Santos1 1Instituto de Tecnologia Quimica e Biologica Universidade Nova de Lisboa Oeiras Portugal 2Department of Chemistry University of Southampton UK Heteronuclear NMR relaxation measurements and hydrogen exchange data have been used to characterize protein dynamics in the presence or absence of stabilizing solutes from hyperthermophiles. Rubredoxin from Desulfovibrio gigas was selected as a model protein and the effect of diglycerol phosphate on its dynamic behaviour was studied. The presence of 100 mM diglycerol phosphate induces a fourfold increase in the half-life for thermal denaturation of D. gigas rubredoxin Lamosa P. Burke A. Peist R. Huber R. Liu . Silva G. Rodrigues-Pousada C. LeGall J. Maycock C. Santos H. 2000 Appl. Environ. Microbiol. 66 1974-1979 . A model-free analysis of the protein backbone relaxation parameters shows an average increase of generalized order parameters of reflecting a small overall reduction in mobility of fast-scale motions. Hydrogen exchange data acquired over a temperature span of 20 C yielded thermodynamic parameters for the structural opening reactions that allow for the exchange. This shows that the closed form of the protein is stabilized by an additional kJ-mol-1 in the presence of the solute. The results seem to indicate that the stabilizing effect is due mainly to a reduction in mobility of the slower larger-scale motions within the protein structure with an associated increase in the enthalpy of interactions. Keywords chemical exchange compatible solutes protein dynamics rubredoxin thermostability. Protein stability activity and dynamics are interrelated issues with great importance not only in physiological .

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