Ryan T A, Myers J, Holowka D, Baird B, Webb W W
Department of Physics, Cornell University, Ithaca, NY 14853.
Science. 1988 Jan 1;239(4835):61-4. doi: 10.1126/science.2962287.
Strong steric interactions among proteins on crowded living cell surfaces were revealed by measurements of the equilibrium spatial distributions of proteins in applied potential gradients. The fraction of accessible surface occupied by mobile surface proteins can be accurately represented by including steric exclusion in the statistical thermodynamic analysis of the data. The analyses revealed enhanced, concentration-dependent activity coefficients, implying unanticipated thermodynamic activity even at typical cell surface receptor concentrations.
通过测量施加电势梯度下蛋白质的平衡空间分布,揭示了拥挤活细胞表面蛋白质之间强烈的空间相互作用。通过在数据的统计热力学分析中纳入空间排斥,可以准确表示可移动表面蛋白质占据的可及表面分数。分析揭示了增强的、浓度依赖性的活度系数,这意味着即使在典型的细胞表面受体浓度下也存在意外的热力学活性。