Related topics: protein

Searching the COVID-19 spike protein for a potential vaccine

The virus that causes COVID-19 is studded on its exterior with "spike proteins," a key component in its ability to infect human cells. Two University of Georgia researchers, Rob Woods and Parastoo Azadi, are investigating ...

Researchers slash pre-drug screening time from years to days

Researchers at Ben-Gurion University of the Negev (BGU) and The Hebrew University of Jerusalem (HU) have developed a powerful tool that will streamline and accelerate the development of disease therapies, transforming a multi-year ...

Fitting a right hand in a left-handed mitten

Many biomolecules come in two versions that are each other's mirror image, like a left and a right hand. Cells generally use the left-hand version of amino acids to produce proteins, and uptake mechanisms were thought to ...

Multiple modes for selectivity of transmembrane transport

LMU researchers utilized a biophysical approach to understand how bacterial import proteins bind and selectively convey their cargoes across membranes. The results reveal an unexpectedly wide variety of transfer mechanisms.

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Carrier protein

Carrier proteins are proteins that transport a specific substance or group of substances through intracellular compartments or in extracellular fluids (e.g. in the blood) or else across the cell membrane. Some of the carriers are water-soluble proteins that may or may not interact with biological membranes, such as some transporters of small hydrophobic molecules, whereas others are integral transmembrane proteins.

Carrier proteins transport substances out of or into the cell by facilitated diffusion and active transport. Each carrier protein is designed to recognize only one substance or one group of very similar substances. The molecule or ion to be transported (the substrate) must first bind at a binding site at the carrier molecule, with a certain binding affinity. Following binding, and while the binding site is facing, say, outwards, the carrier will capture or occlude (take in and retain) the substrate within its molecular structure and cause an internal translocation, so that it now faces the other side of the membrane. The substrate is finally released at that site, according to its binding affinity there. All steps are reversible.

For example:

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