Related Experiment Video

Updated: Feb 8, 2026

Author Spotlight: Harnessing DNA Barcode Technology to Enhance the Efficiency of Medicinal Plant Identification
08:55

Author Spotlight: Harnessing DNA Barcode Technology to Enhance the Efficiency of Medicinal Plant Identification

Published on: November 1, 2024

2.5K

Allosteric Inhibitor of KRas Identified Using a Barcoded Assay Microchip Platform

Amy M McCarthy1, Jungwoo Kim1, A Katrine Museth1

  • 1The Arthur Amos Noyes Laboratory of Chemical Physics, Division of Chemistry and Chemical Engineering , California Institute of Technology , Pasadena , California 91125 , United States.

Analytical Chemistry
|July 7, 2018
PubMed
Summary

We developed a rapid assay platform using barcoded microchips for screening protein-catalyzed capture agents (PCCs). This high-throughput method significantly reduces time and reagents for analyzing PCC candidates targeting KRas proteins.

More Related Videos

Identifying Inhibitors of the HBx-DDB1 Interaction Using a Split Luciferase Assay System05:55

Identifying Inhibitors of the HBx-DDB1 Interaction Using a Split Luciferase Assay System

Published on: December 21, 2019

7.2K
Genetic Barcoding with Fluorescent Proteins for Multiplexed Applications13:14

Genetic Barcoding with Fluorescent Proteins for Multiplexed Applications

Published on: April 14, 2015

9.8K

Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
8.8K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.7K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

3.1K
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
63.4K
Eukaryotic Transcription Inhibitors01:52

Eukaryotic Transcription Inhibitors

Certain biochemical processes, such as embryonic development and cell growth regulation, depend on the repression of specific genes. DNA binding proteins known as eukaryotic transcription inhibitors regulate the repression of gene expression in eukaryotes. The presence of these inhibitors at the required location and time in the cell is triggered by the presence of hormones and additional signals from other cells.
Eukaryotic transcription inhibitors usually contain two distinct domains, a...
11.0K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
6.6K