2007-2008 Updates
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Active transport proteins
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Figure U1-12.1 The structure of an ABC transporter
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Figure U1-12.2 Structures of two states of ABC transporters
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Figure U1-12.3 Proposed mechanism for import of substrate by ABC transporters
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Figure U1-13.1 Visualization of the tunnels in the three monomers in the asymmetric AcrB trimer
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Figure U1-13.2 Proposed mechanism of drug transport by the RMD transporters
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Protein interactions
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Figure 3-0.1 Changes in binding can lead to relocalization of proteins
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Figure 3-0.2 Protein binding can make reactions more efficient and specific
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Figure 3-0.3 Binding can directly alter the activity of proteins
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Figure 3-1.1 The nature of protein-binding interfaces
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Figure 3-1.2 A peptide–protein interaction
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Figure 3-2.1 The quantitative definition of specificity
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Figure 3-2.2 Specificity is a relative quantity that depends on context
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Figure 3-3.1 A binding isotherm
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Figure 3-3.2 Approximate dissociation constants for typical biological interactions
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Figure 3-4.1 Interactions with the same affinity can have different rates of binding and dissociation
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Figure 3-4.2 Avidity of antibody binding
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Figure 3-4.3 Effect of surface density on binding
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Figure 3-5.1 Range of biological affinities and concentrations
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Figure 3-6.1 Increasing specificity through positive discrimination
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Figure 3-6.2 Increasing specificity through negative and positive discrimination
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Figure 3-6.3 Negative selection enables SH3 domains to specifically recognize proline
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Figure 3-7.1 Positive cooperativity leads to all-or-none assembly
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Figure 3-7.2 Diverse mechanisms for cooperative binding of two ligands to one receptor
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Figure 3-7.3 Cooperative recognition of a tandem phosphotyrosine motif by coupled SH2 domains
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Figure 3-7.4 The effect of positive cooperativity on binding curves
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Figure 3-8.1 Detecting binding partners by co-immunoprecipitation
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Figure 3-8.2 The yeast two-hybrid assay
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Figure 3-8.3 Detecting binding partners by far-Western blotting
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Figure 3-9.1 Detecting protein interactions by fluorescence resonance energy transfer (FRET)
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Figure 3-9.2 Visualizing protein binding with FRET
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Figure 3-9.3 Detecting protein–protein interactions with the protein-fragment complementation (PCA) assay
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Figure 3-10.1 Scatchard analysis
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Figure 3-10.2 Determining binding parameters by surface plasmon resonance (SPR)
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Figure 3-10.3 Determining binding parameters by isothermal calorimetry (ITC)
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Protein phosphatases
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Figure U3-3.1 The structure of the catalytic subunit of the human protein serine/threonine phosphatase PP1
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Figure U3-3.2 Schematic structures of representatives of the main class of protein tyrosine phosphatases in humans
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Figure U3-3.3 The catalytic domain of the cytoplasmic protein tyrosine phosphatase PTP1B
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Figure U3-3.4 The catalytic mechanism of protein tyrosine phosphatases
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Figure U3-4.1 The actions of phosphatases in signaling pathways that lead from the insulin receptor
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