9. Shown below is a binding pocket for a protein with a ligand bound. The ligand interacts with a serine and a valine side chain. HN ligand a. Briefly explain, in terms of Kd, the effect of a mutation that replaces the serine residue with a valine residue. b. Briefly explain, in terms of Kd, the effect of a mutation that alters the ligand (as seen below) binding to the original, unmutated, binding site. :0: ligand 2

9. Shown below is a binding pocket for a protein with a ligand bound. The ligand interacts with a serine and a valine side chain. HN ligand a. Briefly explain, in terms of Kd, the effect of a mutation that replaces the serine residue with a valine residue. b. Briefly explain, in terms of Kd, the effect of a mutation that alters the ligand (as seen below) binding to the original, unmutated, binding site. :0: ligand 2

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 8TYK: Which of the following statements about the allosteric site is true? a. The allosteric site is a...

See similar textbooks

Similar questions

2 A biomolecule has a K_d of 1.6mM. A mutated-version of the same biomoleucel was bound by ligan by THIRTY-FIVE-PERCENT, Ligand=1mM. Find the Kd of mutated protein in mM? Does your result show a disruption of binding of biomoilecule(protein)? Why or why not?
2. A ligand binds more tightly to the folded state (N) of a protein than to the unfolded state (U). Show that the ligand stabilizes the protein and calculate by how much (ΔΔGfold = ?). Please help me find out deltadelta G fold.
7. Which of the following events does NOT take place in/on the RER? a. cleavage of the signal recognition peptide b. biosynthesis of core oligosaccharides for N-linked glycosylation c. Phosphorylation of mannose to give rise to mannose-6-phosphate. d. attachment of a core oligosaccharide to protein via asparagine residues e. cleavage of GTP by SRP receptor
1. The figure above shows some of the more common modifications, such as phosphorylation (1), acetylation or methylation (2), adding sugars or lipids (3,4), or adding another polypeptide (5). There are many other possibilities as well.Find and label each of these on the diagram. How might these modifications affect the protein?
1. Search for the `P06858` a) Give information about the PTM and Processing of this protein. b) Which position has maximum amount of variations? Give details about the variations. (Eg: What kind of variation? Feature ID? Disease association? etc..)
Which of the following statements is false? a. GTP is an energy source during various stages of translation. b. In the ribosome, peptidyl transferase catalyzes peptide bondformation between amino acids. c. When the mRNA code UAA reaches the ribosome, there isno tRNA to bind to it. d. A long polypeptide is cut off the tRNA in the A site so its Metamino acid links to the amino acid in the P site. e. Forty-two amino acids of a protein are encoded by 126nucleotides of the mRNA.
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
4. The strength of ligand-protein binding is a property of the binding site called --------------
2. A mixture of the following amino acids (glu, leu, val, arg, ser, phe) was obtained upon complete hydrolysis of a hexapeptide. a. Edman’s reagent releases leucine b. Hexapeptide with carboxypeptidase releases serine. c. Hexapeptide with trypsin forms a tripeptide A with leucine at the N terminal and tripeptide B with valine at the N terminal. d. Tripeptide A with carboxypeptidase releases arginine and a dipeptide with glutamic acid at C terminal. e. Tripeptide B with chymotrypsin form releases serine and another dipeptide. Give: 1. the amino acid sequence of tripeptide A and B. 2. the amino acid sequence in the above hexapeptide.
1. Use the info of this molecule as well as the attached addendum to demonstrate the flow of genetic information to protein sequence as described by the so-called “Central Dogma” . Clearly indicate the direction of your polynucleotide strands and peptide/protein. ATG GCA TGC AAT AGC TCA TGC 2. What would happen to the amino acid sequence if the underlined nucleotide (C) would change to an A?
7. A segment of a DNA strand consists of ...GCTTAGACCTGA.... (a) Identify the expected nucleotide order in the complementary mRNA (b) Identify the sequence of amino acids coded for by this segment of DNA. (c) Describe the bond that forms during translation to link amino acids together. Identify the functional groups that react and the atoms involved.
An intermediate folding stage seen in protein denaturation or renaturation is called : a) domain b) motif c) subunit d) molten globule Proteins which do not renature spontaneously when denaturation conditions are removed may need the assistance of: a) a prosthetic group b) a higher salt concentration c) a lower temperature d) a chaperone protein The information needed for correct protein folding is encoded in: a) the surrounding molecules b) the protein’s amino acid sequence c) the pH of the aqueous medium d) the electrolyte composition of the aqueous solution