Oh

"OH

"OH

Figure 4.5. DEBS combinatorial library. Colors indicate the location of the engineered carbon(s) resulting from catalytic domain substitutions in module 2 (red),module 5 (green),module 6 (blue), or modules 1,3, or 4 (yellow).

Figure 9.8. The malate dehydrogenase dimer, indicating the location of the active sites in each protein plus the dimer interface. Malate dehydrogenase demonstrates substrate inhibition that has been attributed to subunit interactions and allosteric regulation by citrate, although the crystal structure of the protein reveals the absence of a separate allosteric site for citrate.

Figure 4.5. DEBS combinatorial library. Colors indicate the location of the engineered carbon(s) resulting from catalytic domain substitutions in module 2 (red),module 5 (green),module 6 (blue), or modules 1,3, or 4 (yellow).

Figure 9.12. Subunit contacts in aspartate tran-scarbamoylase show heterologous contacts in the catalytic trimers, isologous contacts between regulatory dimers, and regulatory subunit-catalytic subunit interactions.

Figure 9.10. The quaternary structure of glutamate dehydrogenase reveals a complex array of

Figure 9.10. The quaternary structure of glutamate dehydrogenase reveals a complex array of

Figure 9.13. HINT analysis of interactions between the confactor NAD nicotinamide moiety and surrounding 3-phosphoglycerate dehydrogenase residues. Protein carbons are light gray and NAD carbons are black. Nitrogen atoms are blue and oxygen atoms are red. HINT contours are color coded to represent the different types of noncovaleat interactions as follows: blue = favorable hydrogen bonding and acid-base interactions; green = favorable hydrophobic-hydrophobic interactions; and red = unfavorable acid-acid and base-base interactions. The volume of the HINT contour represents the magnitude of the interactions.

Figure 9.14. HINT analysis of interactions between residues at the interface between two sub-units of 3-phosphoglycerate dehydrogenase. The carbons of the two distinct subunits are colored light and dark gray, respectively. Nitrogen atoms are blue, oxygen atoms are red, and sulfur atoms are yellow. HINT contour maps visually displaying interactions between residues at the subunit interface are color coded according to the type of interaction: blue represents hydrogen bonding and favorable acid-base interactions, green displays favorable hydrophobic-hydrophobic contacts, red indicates unfavorable base-base and acid-acid interactions, and purple indicates unfavorable hydrophobic-polar interactions. The volume of the HINT contour represents the magnitude of the interaction. For the analyzed phosphoglycerate dehydrogenase subunits, HINT indicates that a balance between favorable and unfavorable interactions characterizes the interface.

Figure 9.14. HINT analysis of interactions between residues at the interface between two sub-units of 3-phosphoglycerate dehydrogenase. The carbons of the two distinct subunits are colored light and dark gray, respectively. Nitrogen atoms are blue, oxygen atoms are red, and sulfur atoms are yellow. HINT contour maps visually displaying interactions between residues at the subunit interface are color coded according to the type of interaction: blue represents hydrogen bonding and favorable acid-base interactions, green displays favorable hydrophobic-hydrophobic contacts, red indicates unfavorable base-base and acid-acid interactions, and purple indicates unfavorable hydrophobic-polar interactions. The volume of the HINT contour represents the magnitude of the interaction. For the analyzed phosphoglycerate dehydrogenase subunits, HINT indicates that a balance between favorable and unfavorable interactions characterizes the interface.

Figure 11.2. Architecture of whole receptor, emphasizing the external surface and openings to the ion-conducting pathway on the outer (extracellular) and inner (cytoplasmic) sides of the membrane. The positions of the two a subunits, the binding pockets (asterisks), gate of the closed channel (upper arrow), and the constricting part cf the open channel (lower arrow) are indicated.

Figure 11.2. Architecture of whole receptor, emphasizing the external surface and openings to the ion-conducting pathway on the outer (extracellular) and inner (cytoplasmic) sides of the membrane. The positions of the two a subunits, the binding pockets (asterisks), gate of the closed channel (upper arrow), and the constricting part cf the open channel (lower arrow) are indicated.

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