Noncovalent hydrogen bonds

Particularly interesting is that the mediation of singlet excited-state energy is driven by noncovalent hydrogen-bonding interactions. 

All cellular life today incorporates two processes we will refer to as self-assembly and directed assembly (Fig. 1). The latter involves the formation of covalent bonds by energy-dependent synthetic reactions and requires that a coded sequence in one type of polymer in some way direct the sequence of monomer addition in a second polymeric species. On the other hand, spontaneous self-assembly occurs when certain compounds associate through noncovalent hydrogen bonds, electrostatic forces, and nonpolar interactions that stabilize orderly arrangements of small and large molecules. Three well-known examples include the self-assembly of water molecules into ice, DNA... 

Since the polypeptide chains of collagen are almost completely extended, they cannot be stretched much farther without breaking covalent bonds. The a helix can almost double its length by breaking weak, noncovalent hydrogen bonds. 

The synthesis of noncovalent hydrogen-bonded aggregates can often be accomplished simply by mixing the components in the correct molar ratio in an appropriate solvent (usually chlorinated hydrocarbons such as chloroform). In some cases, one of the components (usually the cyanuric acids) may be poorly soluble in chloroform in these cases it may be useful to dissolve the components in a more polar solvent or solvent mixture (e.g. chloroform-methanol), then remove this solvent and redissolve the residue in chloroform. This procedure can overcome kinetic limitations to formation of aggregates associated with solubilities. 

Side chains of the amino acids participate in tertiary (3°) structure, that is, they stabilize the overall conformation of the protein molecule. The forces which hold tertiary structure together include covalent (disulfide bridges) and noncovalent (hydrogen bonding, salt bridge, hydrophobic) interactions. Shapes of tertiary structure subunits can be globular or fibrous. 

Fig. 5. Protein folding. The unfolded polypeptide chain coUapses and assembles to form simple stmctural motifs such as -sheets and a-hehces by nucleation-condensation mechanisms involving the formation of hydrogen bonds and van der Waal s interactions. Small proteins (eg, chymotrypsin inhibitor 2) attain their final (tertiary) stmcture in this way. Larger proteins and multiple protein assembhes aggregate by recognition and docking of multiple domains (eg, -barrels, a-helix bundles), often displaying positive cooperativity. Many noncovalent interactions, including hydrogen bonding, van der Waal s and electrostatic interactions, and the hydrophobic effect are exploited to create the final, compact protein assembly. Further stmctural...

The following sections contain a review of many of the varied synthetic systems that have been developed to date utilising noncovalent interactions to form assembhes of molecules. These sections are loosely demarcated according to the most important type of noncovalent interactions utilized in conferring supramolecular order (ie, van der Waal s interactions, electrostatic interactions, and hydrogen bonds). For extensive reviews, see References 1,2,4—6,22,46,49,110—112. Finally, the development of self-assembling, self-replicating synthetic systems is noted. 

Chemists often call upon certain chemical types of interaction to account for solvent-solvent, solvent-solute, or solute-solute interaction behavior, and we should eon-sider how these ehemical interactions are related to the long-range noncovalent forces discussed above. The important chemical interactions are charge transfer, hydrogen bonding, and the hydrophobic interaction. 

If the protein of interest is a heteromultimer (composed of more than one type of polypeptide chain), then the protein must be dissociated and its component polypeptide subunits must be separated from one another and sequenced individually. Subunit associations in multimeric proteins are typically maintained solely by noncovalent forces, and therefore most multimeric proteins can usually be dissociated by exposure to pEI extremes, 8 M urea, 6 M guanidinium hydrochloride, or high salt concentrations. (All of these treatments disrupt polar interactions such as hydrogen bonds both within the protein molecule and between the protein and the aqueous solvent.) Once dissociated, the individual polypeptides can be isolated from one another on the basis of differences in size and/or charge. Occasionally, heteromultimers are linked together by interchain S—S bridges. In such instances, these cross-links must be cleaved prior to dissociation and isolation of the individual chains. The methods described under step 2 are applicable for this purpose. 

Several different kinds of noncovalent interactions are of vital importance in protein structure. Hydrogen bonds, hydrophobic interactions, electrostatic bonds, and van der Waals forces are all noncovalent in nature, yet are extremely important influences on protein conformations. The stabilization free energies afforded by each of these interactions may be highly dependent on the local environment within the protein, but certain generalizations can still be made. 

Noncovalent synthesis of organic nanostmctures, hydrogen-bonded ensembles including heterocyclic analogs of calix[4]arenes 98PAC1459. 

Hydrogen bonding responsible for stabilization of dimers ., noncovalent weak interactions... 

When thinking about chemical reactivity, chemists usually focus their attention on bonds, the covalent interactions between atoms within individual molecules. Also important, hotvever, particularly in large biomolecules like proteins and nucleic acids, are a variety of interactions between molecules that strongly affect molecular properties. Collectively called either intermolecular forces, van der Waals forces, or noncovalent interactions, they are of several different types dipole-dipole forces, dispersion forces, and hydrogen bonds. 

Crego-Calama M, Reinhoudt DN, ten Cate MGJ (2005) Templation in Noncovalent Synthesis of Hydrogen-Bonded Rosettes. 249 in press Crepy KVL, Imamoto T (2003) New P-Chirogenic Phosphine Ligands and Their Use in Catalytic Asymmetric Reactions. 229 1-40 Cristau H-J, see Taillefer M (2003) 229 41-73... 

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