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Protein combining or protein complementing is a dietary theory for protein nutrition that purports to optimize the biological value of protein intake. According to the theory, individual vegetarian and vegan foods may provide an insufficient amount of some essential amino acids, making protein combining with multiple complementary foods necessary to obtain a meal with "complete protein".
Within the field of molecular biology, a protein-fragment complementation assay, or PCA, is a method for the identification and quantification of protein–protein interactions. In the PCA, the proteins of interest ("bait" and "prey") are each covalently linked to fragments of a third protein (e.g. DHFR, which acts as a "reporter").
There are three principal classes of macronutrients: carbohydrate, protein and fat. [1] Macronutrients are defined as a class of chemical compounds which humans consume in relatively large quantities compared to vitamins and minerals which provide humans with energy.
Natural protein concentrates (often used in bodybuilding or as sports dietary supplements): Soy protein isolate (prepared with sodium or potassium): 80.66; Whey protein isolate: 79; Egg white, dried: 81.1; Spirulina alga, dried: 57.45 (more often quoted as 55 to 77) Baker's yeast: 38.33; Hemp husks 30
Complement control proteins are proteins that interact with components of the complement system. The complement system is tightly regulated by a network of proteins known as "regulators of complement activation (RCA)" that help distinguish target cells as "self" or "non-self."
The foodstuffs listed for comparison show the essential amino acid content per unit of the total protein of the food, 100g of spinach, for example, only contains 2.9g of protein (6% Daily Value), and of that protein 1.36% is tryptophan. [2] [7] (note that the examples have not been corrected for digestibility)
Structure of mannose in its α-D mannopyranose form. Mannan is a polymer of mannose.. The lectin pathway or MBL pathway is a type of cascade reaction in the complement system, similar in structure to the classical complement pathway, [1] in that, after activation, it proceeds through the action of C4 and C2 to produce activated complement proteins further down the cascade.
Protein-fragment complementation assays are often used to detect protein–protein interactions. The yeast two-hybrid assay is the most popular of them but there are numerous variations, both used in vitro and in vivo. Pull-down assays are a method to determine the protein binding partners of a given protein. [26]
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