Substrate concentration how reaction rate (velocity) varies with substrate concentration. Rate increases Answer Bank Rate decreases Rate is unchanged
Q: Indicate the net charge of cysteine at pH 9.5
A: There are four classes of biological macromolecules- proteins, nucleic acids, lipids and…
Q: Consider the O2 binding curve shown below for hemoglobin under normal physiological conditions. In…
A: Oxygen dissociation curve is the graphical representation of effect of partial pressure of oxygen on…
Q: Suppose Gina climbs a high mountain where the oxygen partial pressure in the air decreases to 70…
A: Consider the following reaction: where P is the protein, L is the ligand, PL is the protein-ligand…
Q: Suppose that you are working with an enzyme that has an ionizable active site residue with a pk of…
A: First let's name the curves as shown below, so that we can identify each of them using these…
Q: 2. Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show in…
A: Recall that:Amino acid sequences are written with N-terminal amino acid on the left and C-terminal…
Q: Consider an alpha-helix comprised of twelve amino acid residues. How many hydrogen bonds should be…
A: Proteins are linear polymers of amino acids which form the basic unit. Amino acids consist of a…
Q: Answer the following problem and show your detailed solution and explanation. Cysteine is a…
A: 1.Titration of the Amino Group:The amino group (-NH2) in cysteine has a pKa around 9, so it will be…
Q: Classify each peptide chain as part of a parallel β sheet, part of an antiparallel β sheet, either…
A: Beta-sheets are one of the most common secondary structures seen within proteins. Several…
Q: Why does a folded mutant protein aggregate rather than remain a misfolded monomer?
A: Proteins are essential molecules in biological systems, and their proper folding is crucial for…
Q: Calculate either [H3O+] or [OH-] for each of the solutions at 25 °C. Solution A: [OH¯] = 1.43 × 10¯7…
A: To calculate [H3O+] and [OH-] for each of the solutions, we can use the equation for the ion product…
Q: Which of the following biomolecules is not present in the cell membrane (in any form Proteins O…
A: Biological membranes are bilayered structures that surround the cell or organelle and act as…
Q: = An Fab fragment binds to lysozyme with a dissociation constant of Ka 10-¹1 M. A 1 nM (10-⁹ M)…
A: we can use the equation for the fractional saturation (Y):Y=[F]/Kd+[F]Given:Kd=10−11M[L]=10−9M
Q: Draw the haworth projection of starch (only 2 connected monomers) and cellulose (only 2 connected…
A: Chemically carbohydrates are polyhydroxy aldehydes or ketones. They have the general formula:…
Q: In each case, these are enzymes that catalyze thesame reaction in different species. The question…
A: 1.Aminopeptidases (PR1A from mammal and PR1B from malaria parasite):First, obtain the…
Q: 3. A scientist wishes to find the sequence of a certain protein. Treatment with FDNB releases…
A: In the quest to determine the amino acid sequence of a certain protein, a series of enzymatic…
Q: What is it about alpha helices and beta sheets that would make the coils less flexible?
A: The structure of proteins is a fascinating realm of biology and chemistry. Within the hierarchy of…
Q: The pKas of two hypothetical organic acids are given below: ACOOH ----> ACOO- + H+ (pKa = 4.15)…
A: According to Henderson and Hesselbach equation.PH = Pka + log [A-] /[ HA].So if the acid is soluble…
Q: Draw a diagram of a peptide bond in the cis and trans configurations. Show the contributing…
A: The amino group (NH2) of one amino acid and the carboxyl group (COOH) of another amino acid can join…
Q: The results of a separation using two-dimension gel electrophoresis are shown here. Which protein or…
A: Two-dimensional gel electrophoresis is a technique used in proteomics studies.This technique is…
Q: Compare the stability of the two salt bridges shown circled in blue at pH 8.4. The carboxylate ions…
A: To determine the stability of the two salt bridges at pH 8.4, we need to consider the protonation…
Q: For the equilibrium below, pKa₁ = 7.9 and pKa2 = 10.1. At what pH is [HA] equal to [A²-]?
A: pH of any acid or base tells us its hydrogen ion concentration.PKa- it is that pH when the 50%…
Q: Asp 102 His 57 -H-N [His] [His+] pH = pK₂ + log (AA [HA] = Ser 195 `N----H-O Identify the ways that…
A: Proteases are enzymes that cleave peptide bonds that link two amino acid residues together.…
Q: DNA sense or template DNA sense or template mRNA tRNA protein 5', 3' amino or carboxyl 5' T U A A RG…
A: The genetic information for protein synthesis is stored in DNA. DNA is double-stranded. The…
Q: You dilute 10 µL of your isolated DNA with 90 µL of water. You then measure and record the…
A: To calculate the concentration of the plasmid DNA in μg/mL, we can use the following…
Q: 4. Ionic Forms of Aspartic Acid. Aspartic acid is a triprotic acid that can undergo three…
A: Aspartic acid is a triprotic acid, It can give 3 protons from 3 ionizable groups from the carboxylic…
Q: The shape for curve of oxygen binding to Myoglobin is curve of oxygen binding to Hemoglobin is Flat,…
A: Because of their distinct structure, myoglobin and hemoglobin have slightly different…
Q: What are the chromophores detected by circular dichroism (CD) spectroscopy of a protein? peptide…
A: Circular dichromism (CD) is exhibited by molecules that have a chiral centre. The CD is a reference…
Q: PROTEINS 1. What will happen to free tyrosine after being subjected to xanthoproteic analysis (is it…
A: Proteins are large, complex biomolecules composed of multiple peptide-bonded amino acids. Proteins…
Q: Determine whether each of the examples or phrases describes an essential amino acid, a nonessential…
A: Amino acids are the monomer units of proteins. Out of the 20 general proteogenic amino acids, some…
Q: QUESTION 1 Which of the following concepts in column A best fits the concept in column B.…
A: 1.p-Nitrophenyl α-D-Glucoside - C. Breaks the α-linkages of p-Nitrophenyl α-D-Glucoside, leaving…
Q: Which residue of phenylalanine hydroxylase is phosphorylated? A. Met18 B. Ser16 C. Ser12 D. Tyr24
A: C. Ser12Serine 12 is the residue of phenylalanine hydroxylase that is phosphorylated, and this…
Q: 5. Indicate whether the following amino acid residues would be more likely to be found on the…
A: Protein folding is predominantly dictated by whether a region in a polypeptide chain is composed…
Q: 0.5 M NaOH. Write the acid base reaction that is taking place and use an ICE table to show how the…
A: Number of moles in 100mL of 5M acetic acid can be calculated by the formulaVolume in L ×…
Q: Using a flowchart, illustrate and differentiate the flow of the electrons in the ETC when electrons…
A: NADH produced through glycolysis is present in the cytosol of the cell. The glycolytic pathway is…
Q: can you tell what the pKas are from this unknown amino acid based on buffering regions and narrow…
A: pH = If [H+] concentration in a solution is high, the pH will be low and the solution is acidic. If…
Q: So which form of the arginine side chain is the ionized form? And when the side chain is ionized the…
A: Arginine is an amino acid with a side chain that contains a guanidine group. In its conjugate acid…
Q: The amino acid at the β82 position is in the central cavity that binds 2,3-bisphosphoglycerate in…
A: Asparagine is a neutral amino acid while lysine is positively charged amino acid. Lysine being in…
Q: Match the THE BEST DESCRIPTION with the proper enzyme. RNA Polymerase I RNA Polymerase II RNA…
A: The central dogma of molecular biology is a theory that describes the flow of genetic information in…
Q: Draw a diagram of the hydrogen bonding interactions in: i) a two-stranded antiparallel beta sheet,…
A: Secondary structure of protein: Formed due to twisting of polypeptide chain.The folding is due to…
Q: A receptor-ligand complex has a dissociation constant of Kd = 20 nM. The rate of receptor-ligand…
A: The reverse rate constant (k-1) is a parameter used in chemical kinetics to describe the rate at…
Q: Sequential reaction releases one or more products before all substrates bind the enzyme Answer Bank…
A: In a sequential enzyme catalyzed reactions all substrates bind in a kind of sequential order to its…
Q: A biochemist discovers and purifies a new enzyme, generating the purification table below. Procedure…
A: a) Specific activity =activity(in units)Total Protein(in mg)1. Crude extract =4,000,00020,000=2002.…
Q: Choose any/all that apply to protein synthesis. Ribosomes aid in the formation of peptide bonds…
A: As per the central dogma of molecular biology, genetic information for protein synthesis is stored…
Q: This image shows the tertiary structure of a protein segment. Tertiary structure results from…
A: Ionic bond is formed between a positively charged and a negatively charged group. The charged groups…
Q: Indicate which of the amino acid residues in the following peptide sequence contains a group that…
A: Amino acids are biomolecules that have an amino group and a carboxyl group linked to the same carbon…
Q: What if C-1 of the oxaloacetate were labeled instead, when would the label be released as CO2?
A: Oxaloacetate is a four-carbon compound, and carbon-1 (C-1) refers to the first carbon atom in the…
Q: Please help! Sketch a titration curve of the peptide Ala-Tyr-Gln-Met-Asp-His from pH=0 to 14 up to 5…
A: Titration is used to determine the amount of acid in a solution.Sodium hydroxide or potassium…
Q: 6. A quantitative amino acid analysis reveals that bovine serum albumin (BSA) contains 0.58%…
A: Amino acids, such as glycine, tryptophan, and alanine are organic molecules that contain an amino…
Q: H CH₂ HỎ=CH. CH₂ H₂C (5) H CH₂ H₂C CH₂ CH₂ CH₂ ΝΗ C=NH NH₂ a) Which of the following statements…
A: Recall that:amino acid sequences are written with N-terminal amino acid on the left and C-terminal…
Q: Matching ◆ Another word for Gibbs Free Energy A. R Side Chain of Amino Acid with Positive charge B.…
A: Spontaneous reactions are those that do not require an input of energy to drive the reaction to…
C7 Q2:
Trending now
This is a popular solution!
Step by step
Solved in 3 steps with 1 images
- Using enzyme kinetics, illustrate the cooperative behavior of allosteric enzymes (plot of reaction velocity versus substrate concentration for instance)Consider the Michaelis-Menten equation, below: Vmaz (S V. k + [S] %3D What is the relationship between changes in substrate concentration and velocity when the concentration of substrate, [S), is well below k7 The S terms cancel out in this equation, so there is no effect of changing substrate concentration. The S] term in the numerator is negligible, so there is no impact of changing substrate concentration. Because the enzyme has reached Vr there is no effect of changing substrate concentrations on enzyme velocity. OThe [S term in the denominator is negligible compared to k There is a linear relationship between substrate concentration and velocity.Which statements are false? Initial velocities of enzyme reactions are best obtained in the absence of product because it simplifies analysis. Initial velocities refer to the velocity of the reaction right after it is initiated. The velocity of the reaction as a function of measuring time are curved just like an isothermal binding curve because of substrate binding to the enzyme. Initial velocities correspond to the pre-steady state condition for free enzyme. Initial velocities can sometimes be measured by spectroscopy such as UV/Vis spectroscopy when monitoring the production of NADH from NAD+. The velocity of the reaction will eventually go to zero. The reaction will reach equilibrium because of the presence of the enzyme. It is always better to use substrate rather than product to measure enzyme kinetics.
- USSE EUSS reaction rate substrate concentration Blue line - Enzyme alone Red line - Enzyme + unknown compound The 4 graphs above represent the change in enzyme kinetics with the individual addition of different compounds that could be categorized as either: allosteric inhibitors, allosteric activators, competitive inhibitors, activators or non-competitive inhibitors. Review the graphs above. Each graph represents the activity of an enzyme and the enzyme + the addition of an unknown compound. By comparing the kinetics of the enzyme alone to the enzyme + unknown, determine what type of compound was added to each of the 4 different solutions to elicit the observed change.Consider an enzyme-catalyzed reaction that follows Michaelis-Menten kinetics with KM =3.0 mmol·dm-3. What concentration of a competitive inhibitor with KI = 20 umol·dm-3 willreduce the rate of formation of product by 50% when the substrate concentration is held at 0.10mmol·dm-3.when saturated with substrate, an enzyme has a maximum initial rate of 110mumoles of substrate converted to product per second. At a substrate concentration of 100mu M, the same enzyme converts substrate to product at a rate of 0.010mmoles/ sec. Assuming that Michaelis - Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2x10^-3M.
- Please note the reaction expression below. Which of the following rate constants describes the breakdown of the enzyme-substrate complex? There may be more than one answer. k₂ E+S OK-2 U k₂ 0 k₁ OK.1 k3 k.3 SES EPE+P K.3 K.₂ k.Sketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single substrate (S) into product (P), where the reaction is spontaneous in the forward direction Overlay the free energy diagram for the uncatalyzed reaction and indicate delta delta G〒 on your sketch: Chemical step is rate limitingPractice Mira Gendy 1 of 1 Directions: This short free-response question requires about 6 minutes to answer. The question is worth 3 points. Read the question carefully and completely. Answers must be written out in paragraph form. Outlines, bulleted lists, or diagrams alone are not acceptable. II Substrate Concentration [S] The graph above shows the initial rate of an enzyme-catalyzed reaction at different substrate concentrations in the presence of a constant concentration of the enzyme. Connect the primary structure of the enzyme to its overall shape. I U x X2 5 Initial Rate of Reaction
- An experiment on enzyme-catalyzed reaction was conducted in the laboratory by a student. Results obtained are summarized in the table below. In all the experiments, the concentration of the enzyme is the same. Substrate Concentration Velocity (pmol) (pmol/min) 1.5 0.21 0.28 4 0.32 6 0.36 0.4 15 0.45 18 0.47 1. Plot or graph these results using the Lineweaver-Burk method. 2. Determine the Km and Vmax values. Show all equations and calculations.Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the Vmax value for this reaction. Report your answer to four significant figures in units of uM/min.assume that for an enzyme immobilized on the surface of a nonporous support material, the external mass-transfer resisitance for substrate is not negligible as compared to the reaction rate.The enzyme is subject to substrate inhibition are multiple states possible?why or why not? could the effectiveness factor be greater than one?