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A combined synopsis/solicitation for a Surface Plasmon Resonance (SPR) - Based Protein Interaction Array System, issued by the Department of the Navy's Office of Naval Research, outlining the technical
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How to fill out Surface Plasmon Resonance (SPR) - Based Protein Interaction Array System - N00173-09-R-TB03

01
Gather all necessary materials, including the SPR instrument, sensor chips, and relevant reagents.
02
Prepare the sensor chip by cleaning and activating its surface according to the manufacturer's instructions.
03
Dilute the protein samples to the appropriate concentrations needed for interaction studies.
04
Apply the protein samples to the prepared sensor chip and allow sufficient time for binding.
05
Wash the sensor chip with a suitable buffer to remove unbound proteins.
06
Measure the SPR response to analyze the interaction between proteins by observing the changes in resonance angle or intensity.
07
Record and analyze the SPR data to determine binding affinities and kinetics.

Who needs Surface Plasmon Resonance (SPR) - Based Protein Interaction Array System - N00173-09-R-TB03?

01
Research institutions studying protein interactions.
02
Biotechnology companies developing therapeutic proteins.
03
Pharmaceutical companies engaged in drug discovery and development.
04
Academic laboratories focusing on biochemical and molecular biology research.
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Light is absorbed by electrons in the sensor chip surface. The result is an intensity loss in the reflected beam which can be detected as a dip in the SPR reflection intensity curve. The shape and location of the dip can then be used to provide information about the surface (Figure 1).
The Biacore system, based on the Surface Plasmon Resonance (SPR) principle, offers advantages such as high sensitivity and the ability to perform solvent corrections. It can detect even weak signals and accurately characterize interactions involving molecules with disparate molecular weights.
Surface plasmon resonance (SPR) has emerged as a powerful optical detection technique for studying the binding behaviour of immobilized ligands and analytes in solution. The technique makes it possible to measure interactions in real time with high sensitivity.
Commercial SPR devices are prohibitively expensive and require consumable sensor chips that fit certain specifications of size, thickness, and so forth.
Biacore™ systems monitor the interaction between two molecules, of which one is attached to the sensor surface and the other is free in solution. A sensorgram is a plot of response against time, showing the progress of the interaction. This curve is displayed for you directly on the computer screen during an analysis.
BIACORE systems exploit surface plasmon resonance (SPR) as the detection principle to monitor the interaction between biomolecules in real time without labeling.
Surface Plasmon Resonance is defined as an optical sensing tool that utilizes the sensing principle of surface plasmon resonance, often implemented on an optical fiber substrate for chemical and biosensing applications in various fields such as life sciences, clinical diagnostics, and environmental monitoring.
Biacore™ systems monitor the interaction between two molecules, of which one is attached to the sensor surface and the other is free in solution. A sensorgram is a plot of response against time, showing the progress of the interaction. This curve is displayed for you directly on the computer screen during an analysis.
General Principle of SPR. Surface plasmon resonance occurs when a photon of incident light hits a metal surface (typically a gold surface). At a certain angle of incidence, a portion of the light energy couples through the metal coating with the electrons in the metal surface layer, which then move due to excitation.
System Costs: High-throughput SPR systems with enhanced sensitivity and advanced data analysis tools typically range from $200,000 to $500,000.

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The Surface Plasmon Resonance (SPR) - Based Protein Interaction Array System - N00173-09-R-TB03 is a specialized system used to study biomolecular interactions in real-time without the need for labeling. It uses the principle of surface plasmon resonance to detect changes in the refractive index near a sensor surface, allowing researchers to analyze the binding kinetics, affinity, and overall interaction characteristics of proteins.
Entities that are developing, manufacturing, or utilizing the Surface Plasmon Resonance (SPR) - Based Protein Interaction Array System - N00173-09-R-TB03, including academic institutions, research organizations, and companies in the biotechnology and pharmaceutical sectors, are generally required to file and comply with related documentation or regulations.
To fill out the Surface Plasmon Resonance (SPR) - Based Protein Interaction Array System - N00173-09-R-TB03, you should start by providing details about the research objectives, the specific applications of the SPR system, and a comprehensive breakdown of the experimental procedures to be implemented. Additionally, include relevant data on the interactions being studied, required materials, and methods of analysis.
The purpose of the Surface Plasmon Resonance (SPR) - Based Protein Interaction Array System - N00173-09-R-TB03 is to facilitate the analysis of protein interactions in real-time for a variety of applications such as drug discovery, vaccine development, and understanding fundamental biological processes. It enables researchers to obtain kinetic data on binding events and characterizes interactions in a label-free environment.
The information that must be reported on the Surface Plasmon Resonance (SPR) - Based Protein Interaction Array System - N00173-09-R-TB03 includes a detailed description of the experimental setup, the types of interactions being measured, the protein concentrations used, conditions of the experiment (such as temperature and pH), as well as any relevant results obtained from the interactions, including kinetic and affinity data.
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