Heparin, a highly negatively charged glycosaminoglycan, is used clinically as an anticoagulant. It acts by binding several plasma proteins, including antithrombin III, an inhibitor of blood clotting. The 1:1 binding of heparin to antithrombin III seems to cause a conformational change in the protein that greatly increases its ability to inhibit clotting. What amino acid residues of antithrombin III are likely to interact with heparin

Positively charged amino acids

Explanation:

Heparin is an acid polysaccharide that has a strong negative charge due to the sulfate groups on its glucosamine residues. This negative charge confers to heparin anticoagulant activity. The negatively charged groups in the heparin molecule can interact with positively charged (basic) residues, such as arginine (Arg) and lysine (Lys) of plasma proteins. For example, it has been shown that lysine amino acid residues of antithrombin III may be involved in the binding with heparin.

one is through turgidity. this occurs before ground tissue ( collenchyma

and sclerenchyma cells) become well

developed to give structural support to the plant as it grows bigger. the xylem

tissue (composed of rigid tissue) of the young

plant render this support and also maintaining osmotic turgidity of the surrounding

plant cells.

there are 35 white marbles

step-by-step explanation:

y- yellow marbles

4y + 5 = 45

subtract 5 from both sides

4y = 40

divide for from both sides

y = 10

plug in 10 to get 40 yellow marbles then subtract by 5 to get 35 marbles

thus there are only 10 yellow marbles