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Image Search Results
Journal:
Article Title: Direct evidence for specific interactions of the fibrinogen ?C-domains with the central E region and with each other
doi: 10.1021/bi700944j
Figure Lengend Snippet: A, B, and C – interactions of the BβN-domains with the αC region, αC-domain, and αC-connector, respectively; D, E, and F - interactions of the βN-domains with the αC region, αC-domain, and αC-connector, respectively; G - interactions of the αC region with the BβN-domains treated with thrombin and thus converted to the βN-domains right on the surface; H - interactions of the αC-domain with the BβN-domains in the presence of 200 µg/ml anti-Bβ1-21 mAb; I – paired bars representing cumulative probabilities of forces >10 pN derived from A and D, B and E, and C and F. The dashed lines show the fitting with Gaussian curves to determine the position of each peak that corresponds to the most probable rupture force.
Article Snippet: The rupture force histograms were fit empirically with
Techniques: Derivative Assay
Journal:
Article Title: Direct evidence for specific interactions of the fibrinogen ?C-domains with the central E region and with each other
doi: 10.1021/bi700944j
Figure Lengend Snippet: A, B, and C - interactions of the αC region with NDSK, desA-NDSK, and desAB-NDSK, respectively; D and E - interactions of the αC-domain with NDSK and desA-NDSK, respectively; F – the same as in E, but in the presence of 200 µg/ml anti-Bβ1-21 mAb. The dashed lines show the fitting with Gaussian curves to determine the position of each peak that corresponds to the most probable rupture force.
Article Snippet: The rupture force histograms were fit empirically with
Techniques:
Journal:
Article Title: Direct evidence for specific interactions of the fibrinogen ?C-domains with the central E region and with each other
doi: 10.1021/bi700944j
Figure Lengend Snippet: A - interactions of the pedestal-bound αC region with the αC region coupled to a bead; B - the pedestal-bound αC-domain with the αC-domain coupled to a bead; C, D, and E – the pedestal-bound αC region, αC-domain, and αC-connector with the αC-connector coupled to a bead, respectively; F - the pedestal-bound αC-domain with the BSA-coated bead (negative control). The dashed lines show the fitting with Gaussian curves to determine the position of each peak that corresponds to the most probable rupture force.
Article Snippet: The rupture force histograms were fit empirically with
Techniques: Negative Control
Journal:
Article Title: Engineering of the Fluorescent-Energy-Conversion Arm of Phi29 DNA Packaging Motor for Single-Molecule Studies
doi: 10.1002/smll.200900467
Figure Lengend Snippet: A) Concentration-dependent fluorescence intensity from the extended fluorescent arm of eGFP-gp16. B, a) Enlarged single-molecule image showing individual immobilized eGFP-gp16 distributed over the observed area (70 × 70 μm). b) Point-spread-function fitting of the circled fluorescent spot. The pixel size is 160 nm. C) Photobleaching step analysis showing a) one- or b) two-step drop from the immobilized eGFP-gp16. Time 0 indicates the beginning of laser excitation. D) Distribution of fluorescence intensity of the spots that showed one (solid bars) or two (shaded bars) steps in photobleaching, respectively. Xc represents the peak value obtained from each superimposed Gaussian plot over the data points, with Xc = 5.86 (solidline) for those spots containing one gp16 molecule and Xc = 10.53 (dashed line) for those containing two gp16 molecules.
Article Snippet: A
Techniques: Concentration Assay, Fluorescence