A protein is allosterically regulated by a molecule. This molecule enhances the binding affinity, and is different from the normal ligand. How would you describe this molecule?  A negative homotropic molecule A negative heterotropic molecule A positive heterotropic molecule A positive homotropic molecule

Q: Which of the following must be true based on the data below for ligand L binding to protein A and to…

A: Proteins are biomolecules which catalyzes most of the biochemical reactions in all living cells and…

Q: (c) Outline how you would investigate whether BCMAP would be an effective inhibitor for the protein…

A: Inhibitors are the molecules that slow down or completely block the protein activity of molecules,…

Q: BME (high concentration) disrupts O Disulfide linkages Accelerating disulfide cross-linking. Olonic…

A: BME stands for beta-mercaptoethanol. It is a chemical compound. It can act as a biological…

Q: For a protein that binds multiple ligands with negative cooperativity, which of the following is…

A: The ligand binds to its target molecule

Q: The figure shows binding curves for two proteins that bind the same ligand. Which binding curve…

A: Ligand binding curve: this is also called as saturation curve that shows the fraction Y of protein…

Q: Blueberries have proanthocyanidins, which contain catechin monomer, dimer, and trimer, and polymers…

A: Cells produce lots of oxidants and acidic components when they are performing metabolism.…

Q: 1) A ligand-binding protein showing negative homotropic cooperativity? a) should give an nH value…

A: Cooperativity or cooperative binding occurs when binding of one molecule influences the affinity of…

Q: Which of the following amino acid categories probably would most prefer to be in the middle region…

A: Cell membrane is made up of phospholipids and proteins. Phospholipids are made up of head and…

Q: Are the amino acid residues at the active site need to be in close proximity to one another…

A: Enzymes are the catalysts that catalyze biochemical reactions. These are proteinaceous in nature as…

Q: Two proteins bind the same ligand, and the data is shown below. Select the best answer based on this…

A: A single biomolecule's 2binding affinity is the potency of the binding relationship with its ligand…

Q: Choose ONE of the bond types listed below which most accurately describes the bonds involved in…

A: Proteins are macromolecules that are made up of amino acids. Amino acids are the basic structural…

Q: A pyrimidine(s) with a H-bond acceptor its middle position is/are a Cytosine b Uracil c…

A: Hydrogen bond donor is  the atom that do not provide a hydrogen atom  for hydrogen bonding. They…

Q: Electrophoresis is the movement of molecules within a matrix (paper, gel) to which an electric field…

A: Amino acids are molecules composed of an alpha carbon bonded to to 4 valencies. They are;…

Q: Specificity of protein/protein and protein/DNA binding is determined by what? O Non-covalent bonds O…

A: Introduction Protein, nucleic acid, lipids and carbohydrate are four biomolecules of our body.…

Q: Drag each of the following items into the corresponding boxes to indicate the protein structural…

A: Protein is a three dimensional structure formed by amino acids that polymerizes to form a…

Q: The substitution of a Glutamate residue for Valine residue is a conservative substitution. True…

A: Glutamate and Valine are amino acids. Amino acids are biomolecules that have an amino group, a…

Q: The linkage between individual nucleotides in DNA is known as a phosphodiester bond because—…

A: DNA is made up of nucleotides. Each nucleotide contains a phosphate group, a sugar group, and a…

Q: A DNA sample is found to contain 15% A residues. Use Chargaff's rules to estimate the percent G…

A: DNA is always present in double-stranded form except for some viruses.

Q: The Figure should illustrate the interactions made between the key components of (a) total and (b)…

A: There are two ways by which a ligand would bind to its receptor molecule namely specific & non…

Q: Based on the Hill Plot below, this protein-ligand interaction displays log Y 1-Y 2.5 0 -2.5 -2.5…

A: Hill equation developed by Archibald Hill in 1910 quantitatively describing cooperative ligand…

Q: Would you consider the formation of a peptide bond to be an example of a neutralization reaction?…

A: Introduction : Aminoacids are the building blocks of the proteins. Many aminoacid link with each…

Q: The naturally occurring opioid met-enkephalin is a peptide with the structure Tyr- Gly-Gly-Phe-Met.…

A: Amino acids are zwitterions having both positive and negative charges at neutral pH. The net charge…

Q: Other proteins, such as antibodies, have polypeptide subunits that behave differently.  They lose…

A: Proteins are polymers of amino acids linked by peptide bonds (covalent) by condensation reaction…

Q: I'm working on the thermodynamics of protein binding but I want to understand more on the enthalpic…

A: Introduction Protein folding and protein-ligand interaction are basically thermodynamically driven…

Q: An amino acid has an R-group that is negatively charged at cellular pH. Which of the following…

A: Question - . An amino acid has an R-group that is negatively charged at cellular pH. Which of the…

Q: Two proteins bind the same ligand, and the data is shown below. What is the KD value for Protein B?…

A: The answer of the above question is: Correct answer not given. KD is the equilibrium dissociation…

Q: Imagine that you were asked to denature a protein; you know you can do so using urea.  Your protein…

A: Denaturation is the process by which a protein looses it native structure, to the level that protein…

Q: Non polar Molecules are water soluble. True or false?

A: Non polar molecules  : There is equal sharing of electrons between the atoms of the molecule , hence…

Q: oligosaccharides are attached to proteins for a variety of reasons. They’re attached to the newly…

A: Macromolecules are large organic molecules composed of thousands of covalently connected atoms and…

Q: In an NMR experiment, if a ligand is added to a protein and formed a ligand-protein complex, almost…

A: Chemical shift perturbation is a common technique for demonstrating ligand binding to proteins,…