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Figure 2-1 The functions of tubulin
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Figure 2-2 Substrate binding to anthrax toxin lethal factor
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Figure 2-3 Schematic of the active site of mandelate racemase showing substrate bound
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Figure 2-4 Tight fit between a protein and its ligand
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Figure 2-5 HIV protease, an enzyme from the virus that causes AIDS, bound to three different inhibitors
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Figure 2-6 Differences in the temperature dependence of the specific activity of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from two organisms
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Figure 2-7 Example of a large conformational change
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Figure 2-8 The complex between human growth hormone and two molecules of its receptor
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Figure 2-9 Two protein-DNA complexes
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Figure 2-10 Structure of bacterial cytochrome P450 with its substrate camphor bound
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Figure 2-11 Structure of the dimeric bacterial enzyme 3-isopropylmalate dehydrogenase
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Figure 2-12 Surface view of the heme-binding pocket of cytochrome c6, with hydrophobic residues indicated in yellow
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Figure 2-13 Partner swapping in a signaling pathway
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Figure 2-14 Domain swapping in the papilloma virus capsid protein
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Figure 2-15 Ligand binding involving hydrophobic and hydrogen-bond interactions
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Figure 2-16 Structure of the 50S (large) subunit of the bacterial ribosome
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Figure 2-17 Structure of collagen
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Figure 2-18 The Ste5p scaffold
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Figure 2-19 The enzyme orotidine 5'-monophosphate decarboxylase catalyzes the transformation of orotidine 5'-monophosphate to uridine 5'-monophosphate
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Figure 2-20 Table of the uncatalyzed and catalyzed rates for some representative enzymatic reactions
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Figure 2-21 Energetics of catalysis
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Figure 2-22 The electrostatic potential around the enzyme Cu,Zn-superoxide dismutase
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Figure 2-23 Schematic diagram showing some of the ways in which electrostatic interactions can influence the binding of a ligand to a protein
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Figure 2-24 Schematic diagram of the active site of E. coli aspartate aminotransferase
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Figure 2-25 Catalysis of the reaction of carbamoyl phosphate and aspartate by the enzyme aspartate transcarbamoylase depends on holding the substrates in close proximity and correct orientation in the active site
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Figure 2-26 The pericyclic rearrangement of chorismate to prephenate via the proposed "chair-like" transition state
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Figure 2-27 Effect of binding energy on enzyme catalysis
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Figure 2-28 The active site of citrate synthase stabilizes a transition state with a different geometry from that of the substrate
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Figure 2-29 Phosphoglycerate kinase (PGK) undergoes a conformational change in its active site after substrate binds
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Figure 2-30 NAD-dependent lactate dehydrogenase has a mechanism for excluding water from the active site once substrates are bound
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Figure 2-31 Examples of oxidation/reduction reactions
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Figure 2-32 Examples of addition/elimination reactions
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Figure 2-33 Examples of peptide and phosphoester hydrolysis
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Figure 2-34 Example of the decarboxylation of a carboxylic acid
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Figure 2-35 Table of pKa values for some common weak acids in biology
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Figure 2-36 Active site of lysozyme
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Figure 2-37 Table of organic cofactors
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Figure 2-38 Table of metal-ion cofactors
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Figure 2-39 The coenzyme lysine tyrosylquinone
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Figure 2-40 The chemical steps in peptide hydrolysis catalyzed by the serine protease chymotrypsin
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Figure 2-41 The phosphoenzyme–substrate intermediate in the active site of beta-phosphoglucomutase from Lactococcus lactis
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Figure 2-42 The reaction catalyzed by isocitrate dehydrogenase
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Figure 2-43 The bifunctional enzyme, AICAR transformylase-IMP cyclohydrolase (ATIC) is a single enzyme with two distinct active sites
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Figure 2-44 The two active sites of the bifunctional enzyme tryptophan synthase are linked by an internal channel
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Figure 2-45 Three consecutive reactions are catalyzed by the three active sites of the enzyme carbamoyl phosphate synthetase
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