研究蛋白质-配体相互作用的现代生物物理方法

P. Biswas
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引用次数: 1

摘要

蛋白质-配体相互作用是理解大多数生物相互作用的关键。蛋白质和细胞分子之间相互作用的研究导致了控制生物系统的各种重要途径的建立和鉴定。在生物科学不同领域工作的研究人员对这一领域有着内在的兴趣,并通过应用不同的生物物理方法和工具来量化蛋白质与配体的相互作用,包括蛋白质与小分子、蛋白质与dna、蛋白质与rna、蛋白质与蛋白质在体外和体内的相互作用来补充他们的发现。在本文中,将讨论可用于研究这种相互作用的各种生物物理技术。除了天然凝胶电泳和基于荧光的方法,更多的细节将被讨论,在广泛的现代生物物理工具,如圆二色,傅里叶变换红外(FTIR)光谱,等温滴定量热法,分析超离心,表面等离子体共振,荧光相关光谱,差示扫描荧光法,核磁共振,质谱,单分子光谱,双偏振干涉法,微尺度热泳术和电开关生物传感器,可用于研究蛋白质-配体相互作用的不同方面。
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Modern Biophysical Approaches to Study Protein–Ligand Interactions
Protein–ligand interactions act as a pivot to the understanding of most of the biological interactions. The study of interactions between proteins and cellular molecules has led to the establishment and identification of various important pathways that control biological systems. Investigators working in different fields of biological sciences have an intrinsic interest in this field and complement their findings by the application of different biophysical approaches and tools to quantify protein–ligand interactions that include protein–small molecules, protein–DNA, protein–RNA, protein–protein both in vitro and in vivo. In this paper, the various biophysical techniques that can be employed to study such interactions will be discussed. In addition to native gel electrophoresis and fluorescence-based methods, more details will be discussed, on the broad range of modern day biophysical tools such as Circular Dichroism, Fourier Transform Infrared (FTIR) Spectroscopy, Isothermal Titration Calorimetry, Analytical Ultracentrifugation, Surface Plasmon Resonance, Fluorescence Correlation Spectroscopy, Differential Scanning Fluorimetry, Nuclear Magnetic Resonance, Mass Spectroscopy, Single Molecule Spectroscopy, Dual Polarization Interferometry, Micro Scale Thermophoresis and Electro–switchable Biosensors that can be used to study the different aspects of protein–ligand interactions.
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