Biological interactions noncovalent forces

Noncovalent interactions are central to many key biological functions. The self-assembly of the plasma and organelle membranes, association between receptors and ligands, and folding of RNA and protein molecules are all controlled by noncovalent interactions. Noncovalent forces in the design of proteins have proved useful in gaining insight into... 

The native, biologically active form of a protein molecule is held together by a delicate balance of noncovalent forces hydrophobic, ionic, van der Waals interactions, and hydrogen bonds. In addition,... 

Strong and weak attractive forces between atoms are the glue that holds them together in individual molecules and permits interactions between different biological molecules. Strong forces form a covalent bond when two atoms share one pair of electrons ( single bond) or multiple pairs of electrons ( double bond, triple bond, etc.). The weak attractive forces of noncovalent interactions are equally important in... 

Non-covalent interactions (also called noncovalent forces or noncovalent bonds) are weak interactions between ions, molecules, and parts of molecules. They help shape individual molecules and groups of molecules and ions, but are weak enough to be continually broken and re-formed in the dynamic molecular interplay that is life. In fact. Figure 2.1 shows that biologically important noncovalent interactions are 10-100 times weaker than covalent bonds. 

Macromolecular recognition is ubiquitous in living organisms, and it plays a central role in all biological processes. Proteins specifically interact with other proteins and nucleic acids to form a wide variety of assemblies, from binary complexes to the elaborate multicomponent machines that perform many of the cellular functions.The interaction can be transient, which is the rule in processes such as catalysis or signal transduction, or it can be permanent and build stable assemblies. In either case, it depends on two macromolecules associating to form an interface held by noncovalent forces similar to the forces that stabilize the conformation of the component macromolecules. 

Finally, mastering secondary noncovalent interactions is important not only for supramolecular chemistry and crystal engineering, but controlling these forces is fundamental in the context of an understanding of complex biological processes, particularly the principles and mechanisms of molecular recognition [1-3],... 

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