Laberge M
Johnson Research Foundation, Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia 19104, USA.
Biochim Biophys Acta. 1998 Aug 18;1386(2):305-30. doi: 10.1016/s0167-4838(98)00100-9.
Knowledge of the interactions involving charged, polar and polarizable groups in proteins is fundamental, not only because they are important determinants for gaining insight into biophysical molecular recognition and assembly processes, but also for understanding how the matrix of a protein can be viewed as an electric field capable of inducing Stark perturbations on the spectral properties of biological optical centers. This review describes the essential features of noncovalent interactions in protein systems and discusses the concept of the dielectric constant of a protein in the context of different microscopic and macroscopic modeling approaches. It also provides an account of a specific type of high resolution vibrational and optical Stark spectroscopy attempting to correlate the observed spectral properties of biological optical centers to the intrinsic protein fields induced by the matrix in which they reside.
了解蛋白质中带电、极性和可极化基团之间的相互作用至关重要，这不仅是因为它们是深入了解生物物理分子识别和组装过程的重要决定因素，还因为有助于理解蛋白质基质如何被视为一个能够对生物光学中心的光谱特性产生斯塔克扰动的电场。本综述描述了蛋白质系统中非共价相互作用的基本特征，并在不同的微观和宏观建模方法的背景下讨论了蛋白质介电常数的概念。它还介绍了一种特定类型的高分辨率振动和光学斯塔克光谱，该光谱试图将观察到的生物光学中心的光谱特性与它们所在基质诱导的蛋白质固有场联系起来。
