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Biomacromolecule-ligand interactions

Most physiological processes are the consequences of an effector interaction with biomacromolecules (Harding and Chowdhry, 2001 Weber, 1992), such as interactions between enzymes and their substrates, between hormones and hormone receptors, between antigens and antibodies, between inducer and DNA, and so on. In addition, there are macromolecule-macromolecule interactions such as between proteins (Kleanthous, 2000), between protein and nucleic acid (Saenger and Heinemann, 1989), and between protein and cell-surface saccharide. The effector of small molecular weight is normally referred to as the ligand, and the macromolecular combinant is known as the receptor. [Pg.107]

The biochemical interaction systems are characterized by general ligand interactions at equilibrium, site-site interactions, and cooperativity as well as linkage [Pg.107]

Consider a macromolecular receptor, R, which contains n sites for the ligand L. Each site has the microscopic ligand association constant Kt for the /-site. [Pg.108]

Equilibrium measurement of ligand binding typically yields the moles of ligand bound per mole of macromolecule, v, which is given by [Pg.108]

The solution of v for n-sites gives different expressions under various situations, such as  [Pg.108]


Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful method to determine the structure of biomacromolecules and their complexes in solution. It allows determination of the dynamics of proteins, RNA, DNA, and their complexes at atomic resolution. Therefore, NMR spectroscopy can monitor the often transient weak interactions in the interactome of proteins and the interaction between proteins and small-molecule ligands. In addition, intrinsically unstructured proteins can be investigated, and first reports of structure determination of membrane proteins in the immobilized state (solid state) are developing. This review will introduce the fundamental NMR observables as well as the methods to investigate structure and dynamics, and it will discuss several examples where NMR spectroscopy has provided valuable information in the context of Chemical Biology. [Pg.1269]

Fig. 4 Mobile cyclic compounds enhance molecular recognition. Cyclic compounds can rotate and/or slide along a polymeric chain in the structure of polyrotaxanes, and the mobility of ligands linked by the cyclic compounds play a key role in enhancing multivalent interaction with biomacromolecules. This concept can be used in sugar recognition and plasmid DNA polyplex formation [7]... Fig. 4 Mobile cyclic compounds enhance molecular recognition. Cyclic compounds can rotate and/or slide along a polymeric chain in the structure of polyrotaxanes, and the mobility of ligands linked by the cyclic compounds play a key role in enhancing multivalent interaction with biomacromolecules. This concept can be used in sugar recognition and plasmid DNA polyplex formation [7]...
The optimal situation for an afhnity chromatography is achieved when only the specifically retarded biomacromolecule either remains associated with the immobilized specific ligand until elution is effected by changing the chromatographic condition or is retarded sufficiently to achieve a complete resolution from void volume nonspedlic biomolecules. An important parameter in determining the retardation of a biomacromolecule on an affinity matrix is the dissociation constant, for the interaction of the biomacromolecule, P and the ligand, L ... [Pg.38]

The biochemical applications of UV and visible spectroscopy are determination of concentrations, interactions of ligands with biomaaomolecules and conformational changes caused by experimental perturbations. The sensitivity of UV and visible spectra to the solvent environment of the chromophore leads to shifts in the absorption maximum and the absorption intensity, and it is the basis of solvent perturbation spectra in the structural studies of biomacromolecules (Donovan, 1969). The ideahzed development of environmental (solvent) contribution to the extinction coefficient of a chromophore is described by... [Pg.189]


See other pages where Biomacromolecule-ligand interactions is mentioned: [Pg.107]    [Pg.107]    [Pg.109]    [Pg.107]    [Pg.107]    [Pg.109]    [Pg.34]    [Pg.189]    [Pg.38]    [Pg.198]    [Pg.296]    [Pg.529]    [Pg.31]    [Pg.27]    [Pg.9]    [Pg.256]    [Pg.3]    [Pg.31]    [Pg.86]    [Pg.111]    [Pg.111]    [Pg.104]    [Pg.75]    [Pg.115]    [Pg.128]    [Pg.171]    [Pg.152]    [Pg.143]    [Pg.417]    [Pg.1804]    [Pg.137]    [Pg.44]    [Pg.364]    [Pg.572]    [Pg.1796]    [Pg.233]    [Pg.43]    [Pg.5]    [Pg.39]    [Pg.198]    [Pg.271]    [Pg.282]   
See also in sourсe #XX -- [ Pg.107 , Pg.108 , Pg.109 , Pg.110 ]




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