Hydrogen bond or bridge

The presence of hydrogen bonds to bridging or terminal sulfur atoms... 

While loops lack apparent stmcmral regularity, they exist in a specific conformation stabilized through hydrogen bonding, salt bridges, and hydrophobic interactions with other portions of the protein. However, not all portions of proteins are necessarily ordered. Proteins may contain disordered regions, often at the extreme amino or carboxyl terminal, characterized by high conformational flexibility. In many instances, these disor-... 

The (E)-alkene (74) is formed from Wittig reaction of the corresponding phenyl 3-pyridyl ketone the stereochemical preference is determined by an interaction (either hydrogen bonding or salt bridging) between the carboxylic acid chain being introduced and the amide tether provided by the reactant." ... 

Fig. 62. Three possible pathways (A, B, and C) for heme-heme communication between ct and p2 chains. Hydrogen bonds ( ) or salt bridges and nonbonded packing contacts (—) are indicated. For details, see the text. [Illustrations prepared and copyrighted by I. Geis].

Up to now, we have discussed the primary structure of proteins. The primary structure is the covalently bonded structure of the molecule. This definition includes the sequence of amino acids, together with any disulfide bridges. All the properties of the protein are determined, directly or indirectly, by the primary structure. Any folding, hydrogen bonding, or catalytic activity depends on the proper primary structure. 

Each interface contains 11 or 12 hydrogen bonds or salt bridge interactions. Although the GH/GHR complex buries more surface area into its interface, it stiU contains only 12 specific interactions. Three of the IFN-7/ IFN-7RI interactions occur between mainchain atoms in the AB loop of IFN-7 and the L2 loop of IFN-7RI. In addition to the 12 receptor-cytokine interactions, seven water molecules bridge the donor and acceptor groups of IFN-7 and IFN-7RI via hydrogen bonds (Randal and Kossiakoff, 2001). Since the B-factors for the water and protein atoms in the complex are essentially the same, the water molecules are considered to be an integral part of the interface. The presence of ordered water molecules in the IFN-7/IFN-7RI interface is not likely unique, since the IL-lO/IL-lORl interface is even more polar. However, the poorer diffraction quality of IL-10 complex crystals ( 2.9A versus 2.0A) obtained at this time prevents a detailed description of the interfacial waters. The water molecules in the... 

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