Scott David J
School of Biosciences, University of Nottingham, Sutton Bonington Campus, Sutton Bonington, Leicestershire, LE12 5RD, UK.
Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Oxford, Didcot, Oxfordshire, OX11 0FA, UK.
Biophys Rev. 2016 Nov 22;8(4):441-444. doi: 10.1007/s12551-016-0235-5. eCollection 2016 Dec.
Hydrodynamic studies of the solution properties of proteins and other biological macromolecules are often hard to interpret when the sample is present at a reasonably concentrated solution. The reason for this is that solutions exhibit deviations from ideal behaviour which is manifested as thermodynamic non-ideality. The range of concentrations at which this behaviour typically is exhibited is as low as 1-2 mg/ml, well within the range of concentrations used for their analysis by techniques such as small-angle scattering. Here we discuss thermodynamic non-ideality used previously used in the context of light scattering and sedimentation equilibrium analytical ultracentrifugation and apply it to the Guinier region of small-angle scattering data. The results show that there is a complementarity between the radially averaged structure factor derived from small-angle X-ray scattering/small-angle neutron scattering studies and the second virial coefficient derived from sedimentation equilibrium analytical ultracentrifugation experiments.
当样品存在于浓度适中的溶液中时，蛋白质和其他生物大分子溶液性质的流体动力学研究往往难以解释。原因在于溶液表现出偏离理想行为的情况，这表现为热力学非理想性。这种行为通常表现出的浓度范围低至1-2毫克/毫升，完全在诸如小角散射等技术用于分析的浓度范围内。在这里，我们讨论先前在光散射和沉降平衡分析超速离心的背景下使用的热力学非理想性，并将其应用于小角散射数据的吉尼尔区域。结果表明，从小角X射线散射/小角中子散射研究中得出的径向平均结构因子与沉降平衡分析超速离心实验中得出的第二维里系数之间存在互补性。
