How can I distinguish between orthosteric, allosteric and cryptic ligand binding sites?
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How can I distinguish between orthosteric, allosteric and cryptic ligand binding sites?
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- what is the difference between a ligand and a domain? I understand they both attach with proteins but how do u identify which is which? Also, what is the difference between the function of the two?Under what conditions can a single binding site have a chemical specificity for more than one type of ligand?What is cooperative binding and how can I distinguish positive and negative cooperativity? How does cooperativity amplify the effects of a regulatory molecule?
- Saccharide X, a sugar composed of repeating cellobiose and maltose, is a constituent of two glycoproteins, which are receptors that are found in a certain membrane. For the first glycoprotein, the saccharide is linked by a(1-2) linkages to three sialic acid residues, then O-linked to the glycoprotein. The other glycoprotein, on the other hand, has the saccharide linked by a B(1-3) bond also to three sialic acid residues, then also O-linked to the glycoprotein. Function of 1st glycoprotein – glucose transporter protein Function of 2nd glycoprotein – Na*-K* receptor/ transporter Why is there a difference in the functions of the two glycoproteins?Saccharide X, a sugar composed of repeating cellobiose and maltose, is a constituent of two glycoproteins, which are receptors that are found in a certain membrane. For the first glycoprotein, the saccharide is linked by a(1-2) linkages to three sialic acid residues, then O-linked to the glycoprotein. The other glycoprotein, on the other hand, has the saccharide linked by a B(1-3) bond also to three sialic acid residues, then also O-linked to the glycoprotein. The saccharide was cleaved from its sialic acid residues. The treatments and results are as follows: 1. hydrolysis by B(1-> 4) - disaccharide products 2. hydrolysis by a(1-> 4) - release of 2 disaccharide & 2 monosaccharide units. Show the structure of the saccharide.What is meant by the binding problem, and what is necessary for binding to occur?
- Starting from the situation below, explain the next immediate steps that occur after the agonist ligand binds to the GPCR. Describe what happens in terms of the GTP and the heterotrimeric G protein structure. www www Ligand α В GTP ZAN Y Copyright ©2009 Pearson Education, Inc. GDPAn engineered ligand binds its target with 5 nM affinity at high pH. However, protonation of a histidine residue in the binding site of the ligand renders it unable to bind. Plot the ligand:target complex concentration versus the initial ligand concentration (in protonated or unprotonated form) at pH 4, 5, 6, 7, or 8 (five lines on one plot). Use a total target concentration of 10 nM.Which are the Three binding sites with the same chemical specificity but different affinities for a ligand?
- 1) A ligand-binding protein showing negative homotropic cooperativity? a) should give an nH value less than 1 b) should exhibit a sigmoidal binding curve c) should show a hyperbolic binding curve d) should give an nH value of 1 e) both a and b f) none of the aboveWhich of these situations would produce a Hill plot with a Hill coefficient less than 1? A purified protein is a single polypeptide with two ligand-binding sites, each having a different affinity for the ligand. A purified protein has multiple binding sites, and ligands bind to each site independently without affecting the binding affinity of other sites. A purified protein is a single polypeptide with one ligand-binding site, but the sample is contaminated with some partially denatured protein molecules. A purified protein has multiple binding sites, and ligand binding to one site decreases the affinity of other sites for the ligand.Three different ligands, Ligand Q, Ligand T, and Ligand W, bind to the same protein but with different affinity: The association constant (Ka) for the binding of Ligand Q to the protein is 0.033 nM-1. The fractional saturation (Y) of the protein is 0.20 when the concentration of Ligand T is 1.25 nM. The fractional saturation (Y) of the protein is 0.80 when the concentration of Ligand W is 72 nM. Given this information, Calculate Kd for the binding of each ligand to this protein. Which ligand binds with greatest affinity? Which ligand binds with the lowest affinity?