Ion channels in the context of "Acid–base homeostasis"

Play Trivia Questions online!

 or

Skip to study material about Ion channels in the context of "Acid–base homeostasis"
Ad spacer

⭐ Core Definition: Ion channels

Ion channels are pore-forming membrane proteins that allow ions to pass through the channel pore. Their functions include establishing a resting membrane potential, shaping action potentials and other electrical signals by gating the flow of ions across the cell membrane, controlling the flow of ions across secretory and epithelial cells, and regulating cell volume. Ion channels are present in the membranes of all cells. Ion channels are one of the two classes of ionophoric proteins, the other being ion transporters.

The study of ion channels often involves biophysics, electrophysiology, and pharmacology, while using techniques including voltage clamp, patch clamp, immunohistochemistry, X-ray crystallography, fluoroscopy, and RT-PCR. Their classification as molecules is referred to as channelomics.

↓ Menu

>>>PUT SHARE BUTTONS HERE<<<

👉 Ion channels in the context of Acid–base homeostasis

Acid–base homeostasis is the homeostatic regulation of the pH of the body's extracellular fluid (ECF). The proper balance between the acids and bases (i.e. the pH) in the ECF is crucial for the normal physiology of the body—and for cellular metabolism. The pH of the intracellular fluid and the extracellular fluid need to be maintained at a constant level.

The three dimensional structures of many extracellular proteins, such as the plasma proteins and membrane proteins of the body's cells, are very sensitive to the extracellular pH. Stringent mechanisms therefore exist to maintain the pH within very narrow limits. Outside the acceptable range of pH, proteins are denatured (i.e. their 3D structure is disrupted), causing enzymes and ion channels (among others) to malfunction.

↓ Explore More Topics
In this Dossier

Ion channels in the context of Microbial rhodopsin

Microbial rhodopsins, also known as bacterial rhodopsins, are retinal-binding proteins that provide light-dependent ion transport and sensory functions in halophilic and other bacteria. They are integral membrane proteins with seven transmembrane helices, the last of which contains the attachment point (a conserved lysine) for retinal. Most microbial rhodopsins pump inwards, however "mirror rhodopsins" which function outwards have been discovered.

This protein family includes light-driven proton pumps, ion pumps and ion channels, as well as light sensors. For example, the proteins from halobacteria include bacteriorhodopsin and archaerhodopsin, which are light-driven proton pumps; halorhodopsin, a light-driven chloride pump; and sensory rhodopsin, which mediates both photoattractant (in the red) and photophobic (in the ultra-violet) responses. Proteins from other bacteria include proteorhodopsin.

↑ Return to Menu

Ion channels in the context of Transmembrane domain

A transmembrane domain (TMD, TM domain) is a membrane-spanning protein domain. TMDs may consist of one or several alpha-helices or a transmembrane beta barrel. Because the interior of the lipid bilayer is hydrophobic, the amino acid residues in TMDs are often hydrophobic, although proteins such as membrane pumps and ion channels can contain polar residues. TMDs vary greatly in size and hydrophobicity; they may adopt organelle-specific properties.

↑ Return to Menu
LINKED FROM (PARENTS)
← Microbial rhodopsin ← Acid–base homeostasis ← Transmembrane domain ← Physiological pH
LINKS TO (CHILDREN)
Protein domain → Potassium channel → Phosphorylation → Cell membrane → Membrane protein → Ions → Resting membrane potential → Action potential → Gating (electrophysiology) → Ion → Secretion → Epithelial cell → Cell (biology) → Ionophore → Ion transporter → Biophysics → Electrophysiology → Pharmacology → Voltage clamp → Patch clamp → Immunohistochemistry → X-ray crystallography → Fluoroscopy → RT-PCR → Channelomics →