Figure Menu

Chapters 1–13

Figure 1-3. SH2 domain-containing proteins grouped according to biochemical activity

Figure 2-2. Novitas characterization flowchart

Figure 6-2. GST pull-down assay

Figure 7-2. Flowchart for cross-linking screening

Figure 8-1. Identification of interacting proteins by screening λ phage cDNA expression libraries

Figure 9-1. Engineering of proteins based on structural information

Figure 10-2. Flowchart, controls, and library screen

Figure 12-1. Suppressor strategies

Figure 12-3. Mutant phenotypes for suppressor analysis

Figure 13-1. Schematic of an isothermal titration calorimeter

Figure 13-7. Energy landscape of Ras/Raf contact surface

Chapters 14–20

Figure 14-2. Sedimentation velocity profiles

Figure 14-3. Sedimentation coefficient distribution

Figure 15-1. Time-resolved infrared absorbance difference spectra

Figure 16-1. X-ray structure determination of macromolecules

Figure 17-1. Different pressure regimes in the modified Q-TOF 2 mass spectrometer

Figure 18-1. AP-MS procedure

Figure 19-2. Interaction monitored as a sensorgram

Figure 20-1. HIV-1 attachment and entry into cells

Figure 20-2. SPR-based gp120/Env interaction assays

Figure 20-3. Sensorgram overlays for gp120 JR-FL binding to 17b mAb surface

Chapters 21–25

Figure 21-1. Schematic of AFM

Figure 21-2. Functionalization of AFM tips with ConA

Figure 21-3. Interaction between streptavidin-functionalized tip and biotinylated agarose bead

Figure 22-1. Operation principles of optical tweezers

Figure 22-2. Experimental setup, flow system, and flow cell

Figure 23-2. Concept of spFRET

Figure 24-2. Sequence alignment of ATP-binding site of protein kinases

Figure 24-3. Analog inhibition assay

Figure 25-1. Membrane-based yeast two-hybrid system

Chapters 26–31

Figure 26-1. Bacterial two-hybrid system

Figure 26-2. Cloning strategy and screening/selection procedures for bacterial two-hybrid system

Figure 27-1. Ribosome display

Figure 27-3. Ribosome display construct for assembly PCR

Figure 28-1. Hammerhead ribozyme

Figure 28-2. Ribozymes for detection of protein interactions

Figure 29-2. Matrix and graphic representation of amino acid selectivity data

Figure 30-1. Aptamer analysis of protein interactions

Figure 31-2. Manual SPOT synthesis

Figure 31-5. Classic epitope analysis experiment

Figure 31-6. Dual-positional-scanning peptide library experiment

Chapters 32–35

Figure 32-1. FRET efficiency

Figure 32-2. Acceptor photobleaching experiment

Figure 32-6. FLIM images of live cells

Figure 33-4. GFP PCA-based library screening strategy

Figure 33-5. In vivo β-lactamase PCA applications

Figure 34-1. BiFC assay

Figure 34-5. Multicolor fluorescence complementation analysis

Figure 35-1. Imaging of protein interactions in living animals

Figure 35-2. Imaging in living mice by two-hybrid approach

Chapters 36–40

Figure 36-1. Specimen preparation for EM tomography

Figure 36-9. Manual contouring of membrane structures in tomograms

Figure 37-1. Protein–protein interactions by two-hybrid and MS techniques

Figure 37-5. Array-based screening procedure

Figure 38-1. Overview of TAP method

Figure 39-1. Determining interaction networks mediated by protein recognition modules

Figure 39-4. Comparison of networks obtained by two orthogonal approaches

Figure 40-1. The SGA method

Figure 40-3. SGA screen enriched for genes related to BIM1

Chapters 41–46

Figure 41-1. Computational prediction of protein interaction

Figure 42-1. Physical interactions involving proteins

Figure 42-3. 2358 protein–protein interactions in yeast

Figure 42-4. Kohn's symbols

Figure 44-3. Human GH binding to the receptor

Figure 44-6. Space-filling model of the third α-helix

Figure 45-1. AutoDockTools

Figure 45-2. AutoGrid

Figure 46-1. Regulation of p53 by MDM2

Figure 46-3. X-ray structure of MDM2/Nutlin-2 complex