Novel grafted electrochemical interface for covalent glucose oxidase immobilization using reactive pentafluorophenyl

Margalida Artigues1, Sejin Oh2, Joan Gilabert-Porres2

  • 1Electrochemical Methods Laboratory - Analytical and Applied Chemistry Department at Institut Químic de Sarrià, Universitat Ramon Llull, Via Augusta, 390, 08017, Barcelona, Spain.

Related Concept Videos

What is an Electrochemical Gradient?01:26

What is an Electrochemical Gradient?

Adenosine triphosphate, or ATP, is considered the primary energy source in cells. However, energy can also be stored in the electrochemical gradient of an ion across the plasma membrane, which is determined by two factors: its chemical and electrical gradients.
The chemical gradient relies on differences in the abundance of a substance on the outside versus the inside of a cell and flows from areas of high to low ion concentration. In contrast, the electrical gradient revolves around an...
127.8K
Covalent Bonds01:29

Covalent Bonds

Overview
162.2K
Covalent Bonds01:08

Covalent Bonds

Overview
When two atoms share electrons to complete their valence shells, they create a covalent bond. An atom's electronegativity—the force with which shared electrons are pulled towards an atom—determines how the electrons are shared. Molecules formed with covalent bonds can be either polar or nonpolar. Atoms with similar electronegativities form nonpolar covalent bonds; the electrons are shared equally. Atoms with different electronegativities share electrons unequally,...
10.9K
Network Covalent Solids02:18

Network Covalent Solids

Network covalent solids contain a three-dimensional network of covalently bonded atoms as found in the crystal structures of nonmetals like diamond, graphite, silicon, and some covalent compounds, such as silicon dioxide (sand) and silicon carbide (carborundum, the abrasive on sandpaper). Many minerals have networks of covalent bonds.
To break or to melt a covalent network solid, covalent bonds must be broken. Because covalent bonds are relatively strong, covalent network solids are typically...
16.2K
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.7K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
9.6K