Feedback See Periodic Table Which of the following correctly describe both a lectin and a glycoprotein array? Choose one or more: A. can be used to determine the structure of glycan groups B. can be used to identify interactions between lectins and glycans C. can be used to detect interactions between glycans and antibodies D. can be used with more than one type of biological sample (e.g. glycoproteins and bacteria)
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- Theoretical and experimental measurements show that in many cases, thecontributions of ionic and hydrogen-bonding interactions to ΔH for proteinfolding are close to zero. Provide an explanation for this result..A protein gives a single band on SDS gel electrophoresis, as shown in lanes 1 and 2 below. There is little if any effect from addingSmall molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…
- Will rate ASAP Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? (Assume pK values of each amino acid are equal to the pK value for the free amino acid in solution.) I. leucine II. lysine III. aspartic acid IV. histidine A) I, II, III B) I, II C) I D) II E) I, IIIFor a binding protein to show positive cooperativity…. Choice 1 of 4:the protein must be able to adopt at least 2 different conformations each with different affinities for the ligand Choice 2 of 4:the protein must be able to bind to at least 2 different types of ligand Choice 3 of 4:the protein must bind to one molecule of ligand fast and one molecule of ligand slowly Choice 4 of 4:the Kd must be in the micromolar rangeThe allosteric regulation of ATCase by CTP is an example of: 1. Negative homotropic allostery 2. Positive homotropic allostery 3. Negative heterotropic allostery 4. Positive heterotropic allostery
- Proteoglycan aggregates in tissues form hydrated, viscousgels. Can you think of any obvious mechanical reason whytheir capacity to form gels is important to cell function?[Hint: Liquid water is virtually incompressible.]Calculate the concentration of the ligand required to fill 25% of the binding site. X+A ⇌ XA , ka = 1.5 ×10-6 Y+A ⇌ YA , ka = 4.7 × 10-4 (i.e, q = 0.25) for both proteins.An 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.
- Time le The net negative charge of the heteropolysaccharide chain in proteoglycans causes: Select one: a. Secretion of proteoglycans to extracellular matrix. b. The "slippery" nature of mucus. O c. Targeting of proteoglycans to lysosomes for degradation O d. Specific attachment of the sugar chains to serine residue Clear my choice One of the following functions is not of Nitric Oxide: Select one: a. mediates muscular contractions O b. prevents platelets formation O c. mediates bactericidal actions of macrophages O d. function as neurotransmitter Clear my choice(A) What property of a protein might make it difficult to transfer it from polyacrylamide gel to nitrocellulose? Explain your reasoning. (B) What parameter of the gel transfer protocol can be adjusted that might help improve the transfer of these problematic proteins to the nitrocellulose membrane? Explain your reasoning. (C) How can we check if proteins have been successfully transferred from the polyacrylamide gel to nitrocellulose?ILLUSTRATIONS For each of the given proteins: Draw the final location of the following proteins after being translocated. Label the organelle (as well as the organelle parts/compartments) and the cytosol (if necessary) in order to clearly depict the protein's location and orientation. Label the amino and carboxyl ends of the protein. Below your drawing, indicate: . . a. the receptor/s b. the energy source c. if there is signal peptide cleavage or none E. Mitochondrion H₂N-MTS ITS* "Internal targeting sequence that has no cleavage site -COOH SALE