Interaction,*small

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...

Molecularly motivated empiricisms, such as the solubility parameter concept, have been valuable in dealing with mixtures of weakly interacting small molecules where surface forces are small. However, they are completely inadequate for mixtures that involve macromolecules, associating entities like surfactants, and rod-like or plate-like species that can form ordered phases. New theories and models are needed to describe and understand these systems. This is an active research area where advances could lead to better understanding of the dynamics of polymers and colloids in solution, the rheological and mechanical properties of these solutions, and, more generally, the fluid mechaiucs of non-Newtonian liquids. 

Rahman, G.M.A., et al., Dispersable carbon nanotube/gold nanohybrids evidence for strong electronic interactions. Small, 2005.1(5) p. 527-530. 

All group 10 complexes feature a rather strong M-B interaction. Small, nonregular variations are observed in this triad, with Pd and Pt forming the weakest and strongest interactions, respectively. 

De Haan and de Boer What are the interactions Small amount of Fe bound to... 

This chapter has introduced interaction profiling as a new and powerful approach to understand what interactions small molecules exploit in order to be competitive against ATP and, often, selective for a particular kinase. More importantly, we have shown that the information encoded in the interaction pro-... 

Wang J, Nanomaterial-based amplified transduction of biomolecular interactions, Small, 2005, 1, 1036-1043. 

Since hydrogen-bonding is a hard acid-hard base interaction, small basic anions prefer specific solvation by protic solvents. Hence, the reactivity of F , HO , or CH3O is reduced most on going from a dipolar non-HBD solvent such as dimethyl sulfoxide to a protic solvent like methanol. Dipolar non-HBD solvents are considered as fairly soft compared to water and alcohols [66],... 

The logical and necessary successors to the Human Genome Project, which delivers primary seqnence data, are comparable efforts in bioinformatics (to understand the meaning of the seqnences), in structural studies (to understand the structures and interactions of molecules derived from gene sequences) and the molecular design of interacting (small) molecules as well as (finally ) the overall biological systems for validation, verification and application (e.g., mouse, zebra fish. Drosophila and hnman). ... 

Siomi MC, Sato K, Pezic D, Aravin AA. PlWI-interacting small RNAs the vanguard of genome defence. Nat Rev Mol Cell Biol. 2011 12 246-58. 

Fig. 15. Repulsive potential for 1—1 valent electrolytes as a function of for strong interaction (small rf).

The simpliest case of ENA SEC represents the separation of oligomers. The experimental conditions are selected so that only the end gronps on the oligomer molecule are retained due to the enthalpic interactions. Small molecules are strongly retained and their increase. As the molar mass of oligomer rises, the effect of end groups decreases. This leads to the SEC-like elution order with increased selectivity of separation (see Figure 3(b)). 

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