Hydrogen bonding, hydrophilic amino groups

Among the common amino acids, eleven have side chains that contain polar functional groups that can form hydrogen bonds, such as —OH, —NH2, and — CO2 H. These hydrophilic amino acids are commonly found on the outside of a protein, where their interactions with water molecules increase the solubility of the protein. The other nine amino acids have nonpolar hydrophobic side chains containing mostly carbon and hydrogen atoms. These amino acids are often tucked into the inside of a protein, away from the aqueous environment of the cell. 

Noncovalent interactions play a key role in biodisciplines. A celebrated example is the secondary structure of proteins. The 20 natural amino acids are each characterized by different structures with more or less acidic or basic, hydrophilic or hydrophobic functionalities and thus capable of different intermolecular interactions. Due to the formation of hydrogen bonds between nearby C=0 and N-H groups, protein polypeptide backbones can be twisted into a-helixes, even in the gas phase in the absence of any solvent." A protein function is determined more directly by its three-dimensional structure and dynamics than by its sequence of amino acids. Three-dimensional structures are strongly influenced by weak non-covalent interactions between side functionalities, but the central importance of these weak interactions is by no means limited to structural effects. Life relies on biological specificity, which arises from the fact that individual biomolecules communicate through non-covalent interactions." " Molecular and chiral recognition rely on... 

The NIPA gel has a molecular structure which contains not only hydrophilic (NH, C=0) but also hydrophobic (isopropyl) groups. Recently, Hirotsu [8] investigated the phase transition behavior of NIPA gel/water/alcohol systems and explained the thermoshrinking by the destruction of hydrogen bonds between water molecules and amino or carbonyl groups. However, Ulbrich and Kopecek [9] pointed out the importance of hydrophobic interactions in then-study on the mechanical properties of N-substituted acrylamide gels. 

This porosity which is also retained in the LB films, may explain the water penetration between the 2-D crystallites. The amide groups located at the periphery of these domains generate hydrophilic centers which may retain water molecules by binding via hydrogen bonds. In addition, the hydrophilic head groups, such as a-amino acids or carboxylic acids which (in contrast to the Y-type films), cannot form hydrogen bonded pairs, are free to bind water molecules between the layers. We suggest that when... 

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