Biomacromolecular interactions

Nuclear magnetic Resonance Absorption of radiation giving rise to transitions between different spin orientations of nuclei in a magnetic field N, P, G Sequences of biomacromolecules. Complete 3D structures. Unambiguous detection of certain functioned groups and information about the environment. Structural identification by fingerprinting. Studies of biomacromolecular interactions with ligemds. 

Most biomacromolecular interactions (bindings) involve the formation of some types of noncovalent bond and some specific region of the macromolecule called the binding site. Determinations of equilibrium binding processes are mostly indirect in that either i) the fraction of all of the ligand molecules (generally labeled molecules are used) in the system that are bound or ii) the fraction of binding sites that are occupied, is measured. 

The molecular mechanical approach to simulating biomacromolecular structures by the use of potential energy functions has been discussed. These potential energy functions are an enthalpic contribution to the free energy, but the free energy contains entropic contribution. There are two forms of entropy in a biomacromolecular system namely the conformational entropy, which entails the inherent entropy of the biomacromolecular structure and the solvent entropy, which results from interactions between a biomacromolecule and solvent molecules. 

Figure 14.1 Components of biomacromolecular infonnatics and their interactions...

Fast Mulipole Methods for Calculating Electrostatic Interactions in Biomacromolecular Simulations. 

Przybylski, M. and Glocker, M.O. (1996) Electrospray mass spectrometry of biomacromolecular complexes with noncovalent interactions - new analytical perspectives for supramolecular chemistry and molecular recognition processes. Angew. Chem. Int. Ed., 35, 806-826. 

See also Biomacromolecular Applications of Circular Dichroism and ORD Dyes and Indicators, Uses of UV-Visible Absorption Spectroscopy Macromolecule-Ligand Interactions Studied By NMR Nucleic Acids and Nucleotides Studied Using Mass Spectrometry Nucleic Acids Studied Using NMR Peptides and Proteins Studied Using Mass Spectrometry Proteins Studied Using NMR Spectroscopy. 

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