Tag: Protein binding

According to the National Institutes of Health, only the unbound or "free" fraction of a drug is pharmacologically active and can exert a therapeutic effect. This is precisely why protein-bound drug breakdown, or more accurately, dissociation, is a cornerstone of effective drug therapy and patient safety.

Did you know that the dry, puckering sensation you feel from a strong cup of tea or red wine is a direct result of tannins binding to proteins in your saliva? This common chemical reaction perfectly illustrates what do tannins do to protein, causing them to clump together and precipitate.

Did you know that many vitamins rely on specialized protein carriers to travel through your bloodstream? This transport system is crucial for cellular delivery, and one key protein family, the alpha-2 globulins, plays a significant role. While several substances are carried in this protein fraction, the most definitive answer to which vitamin binds to alpha-2 globulin is Vitamin D.

The interaction between avidin and biotin is one of the strongest non-covalent bonds known in nature, with an exceptionally high affinity. This potent bond makes avidin, a protein found in raw egg whites, the primary antagonist of biotin, a crucial water-soluble B-vitamin.

Polyphenols are a vast group of over 8,000 phytochemicals, and their diverse chemical structures lead to a wide array of reactions. Understanding what are the reactions of polyphenols is crucial for their utilization in food, nutrition, and health, as these reactions can influence color, flavor, and antioxidant capacity.

Up to 90% of the mercury found in fish tissue is in its highly toxic, organic form called methylmercury. This compound is primarily absorbed by the fish's body, where it binds tightly to proteins, and its overall effect is influenced by the mineral selenium.

The human body contains hundreds of proteins capable of binding calcium, with affinities ranging from nanomolar to millimolar concentrations. Understanding **which protein can bind to calcium** is crucial for appreciating the complex nutritional and biological processes that govern everything from strong bones to muscle function. This fundamental interaction ensures calcium is properly managed throughout the body for optimal health.

Approximately 85–90% of all circulating vitamin D metabolites are bound to a specific carrier protein in the bloodstream. This vital transport protein, known as Vitamin D-Binding Protein (DBP), is responsible for carrying vitamin D throughout the body and controlling its availability to various tissues.

Recent structural investigations have revealed that the flavonoid quercetin achieves many of its biological effects by interacting with various protein targets. These interactions can and often do lead to a loss of protein function, especially in the context of enzyme activity.