Related Experiment Video
Updated: Jul 13, 2026
08:46
Electronic Tongue Generating Continuous Recognition Patterns for Protein Analysis
Published on: September 16, 2014
Phosphorylation-driven protein-protein interactions: a protein kinase sensing system
Qunzhao Wang1, David S Lawrence
1Department of Biochemistry, The Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA.
Journal of the American Chemical Society
|May 26, 2005
Summary
Researchers developed a flexible protein kinase sensing system with significant fluorescence changes upon phosphorylation. This system utilizes peptide substrates with environmentally sensitive fluorophores for sensitive and versatile kinase activity detection.
Area of Science:
- Biochemistry
- Molecular Biology
- Chemical Biology
Background:
- Protein kinases are crucial enzymes regulating cellular processes.
- Dysregulated kinase activity is implicated in various diseases, including cancer.
- Sensing kinase activity is vital for biological research and drug discovery.
Purpose of the Study:
- To develop a novel, highly flexible sensing system for protein kinase activity.
- To create a system that exhibits significant fluorescence changes in response to phosphorylation.
- To enable unobtrusive positioning of fluorescent indicators on peptide substrates.
Main Methods:
- Preparation of a library of Src kinase peptide substrates.
- Incorporation of environmentally sensitive fluorophores at various positions.
- Utilizing a phosphotyrosine binding domain protein (Lck SH2 domain) for signal transduction.
Main Results:
- Achieved severalfold changes in fluorescence intensity upon phosphorylation.
- Demonstrated robust fluorescence changes in the presence of the Lck SH2 domain.
- Showcased the ability to position fluorophores unobtrusively on peptide substrates.
Conclusions:
- The developed protein kinase sensing system offers high flexibility and sensitivity.
- The system allows for the use of diverse fluorophores with distinct photophysical properties.
- This technology provides a valuable tool for studying kinase activity and developing kinase-targeted therapeutics.
Related Concept Videos
01:00Enzyme-linked Receptors
Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
01:02Protein Digestion
Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
01:28What are Proteins?
Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight. Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional structure...
01:28Protein Denaturation
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
01:30Modified-Release Drug Delivery Systems: Stimuli-Activated
Stimuli-activated drug delivery systems are designed to release drugs in response to specific physical, chemical, or biological stimuli. These systems often utilize hydrogels—three-dimensional, hydrophilic polymer networks capable of swelling in aqueous environments and retaining significant fluid volumes. Upon exposure to particular stimuli, these hydrogels undergo structural transitions that allow the embedded drug to be released. Due to this adaptive behavior, such systems are also called...
01:30Other Stress Responses in Bacteria
Bacteria have global regulatory systems that control several types of stress mechanisms. These include Pho regulon and the heat shock response, which are essential systems for environmental adaptation, such as nutrient limitation and proteotoxic stress. The Pho regulon and the heat shock response exemplify bacterial resilience, enabling rapid adaptation to fluctuating environmental conditions.Pho RegulonBacteria require phosphorus for essential cellular processes, including nucleic acid...