Biochem I Problem Set 6a(1) (1)

correct answer should be 20.6 but how?

Biochemistry topic question: An enzyme catalyzes a reaction with a with a Km value of 1 × 10–6 M and V max =20mmol/min. At a concentration of 1 × 10–6 M substrate, the rate of the reaction will be: See attached image. Please help. Thank you

I. Buffer Preparation A researcher in Biochemistry is isolating α-glucosidase enzyme from malted wheat flour. The protocol requires the use of 2.00L of 0.225 M of lactate buffer with pH of 4.25. How will he/she prepare this buffer from 2.00 M lactic acid solution and solid sodium lactate (NaC3H5O3) The Ka of lactic acid is 1.38 x 10-4. [ Na=23.0, C=12.0, H=1.01, O=16.0 g/mol]

Quantitative Estimation of Amino Acids by Ninhydrin http://vlab.amrita.edu/?sub=3&brch=63&sim=156&cnt=2 can u help me with question 2 of the assignment questions  Based on the experimental data provided, estimate the amount of amino acid in the given unknown solution by Ninhydrin method. SI No. Volume of standard amino acid solution (ml) Amount of amino acid (µg) OD at 570nm 1 Blank   0 2 0.2   0.12 3 0.4   0.25 4 0.6   0.45 5 0.8   0.55 6 1.0 100 0.68 7 Unknown (0.5ml)   0.41

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P3D.2 In biological cells, the energy released by the oxidation of foods is stored in adenosine triphosphate (ATP or ATP“).The essence of ATP's action is its ability to lose its terminal phosphate group by hydrolysis and to form adenosine diphosphate (ADP or ADP): ATP* (aq) + H,O() → ADP* (aq) + HPO (aq) + H,O*(aq) At pH = 7.0 and 37°C (310K, blood temperature) the enthalpy and Gibbs energy of hydrolysis are A,H =-20kJ mol and A,G=-31 kJ mol", respectively. Under these conditions, the hydrolysis of 1 mol ATP“(aq) results in the extraction of up to 31kJ of energy that can be used to do non- expansion work, such as the synthesis of proteins from amino acids, muscular contraction, and the activation of neuronal circuits in our brains. (a) Calculate and account for the sign of the entropy of hydrolysis of ATP at pH = 7.0 and 310K. (b) Suppose that the radius of a typical biological cell is 10µm and that inside it 1x 10ʻ ATP molecules are hydrolysed each second. What is the power density of…

answer item no. 7-10

[Two - Biomolecules] INSTRUCTIONS — Answer the following multiple-choice questions and EXPLAIN in 3-5 sentences why you chose that answer. — Answer properly

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2.1

answer only question g

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41 The following data describe an enzyme-catalyzed reaction (hydrolysis of carbobenzoxyglycyl-L-tryptophan) Plot these results using the Lineweaver-Burk method, and determine values for KM and Vmax Velocity (mM.sec-) 0 024 0 036 0 053 0 060 0 061 0 062 Substrate Concentration (mM) 25 50 10 0 15 0 200 25 0 42 If the KM of an enzyme for its substrate remains constant as the concentration of the inhibitor increases, what can be said about the mode of inhibition and why? 43 Calculate the turnover number for an enzyme, assumıng Vmax IS 05 M sec1 and the concentration of the enzyme used is 0 002 M Why is it useful to know this? 44 Dıscuss the mechanism of the Bohr effect that occurs during the interactions of Hb with oxygen under physiological conditions in the lungs and tissues Make use of relevant graphs and diagrams to explain your answer

Question: Fatty acid degradation (breakdown) and synthesis have many similarities but are uniquely different.Explain two ways that these pathways are similar and two ways that they differ. Please give four seperate factors in point form. Two similarities and two differences 4 overall.

Question: A. To explore the consequences of coupling ATP hydrolysis under physiological conditions to a thermodynamically unfavorable biochemical reaction, consider the hypothetical transformation X⟶Y, for which Δ?′°=20.0 kJ/mol. What is the ratio of [Y]/[X][Y]/[X] at equilibrium? B. Suppose XX and YY participate in a sequence of reactions during which ATP is hydrolyzed to ADP and Pi. The overall reaction is X+ATP+H2O⟶Y+ADP+Pi Calculate [Y]/[X] for this reaction at equilibrium. Assume that the temperature is 25.0 °C and the equilibrium concentrations of ATP, ADP, and Pi are 1.00 M each. C. We know that [ATP], [ADP], and [Pi] are not 1.00 M under physiological conditions. Calculate [Y]/[X] for the ATP‑coupled reaction when the values of [ATP], [ADP], and [Pi] are those found in rat myocytes. Metabolite               Concentration in rat myocytes (M) ATP                          8.05x10-3 ADP                         0.93x10-3 Pi                             8.05x10-3

Amino acid alanine

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Question:- Based on the figure below, predict what peptide bond could be the substrate of each protease(The bond marked in blue is where hydrolysis occurs, choose 2 peptides per protease type) Chymotrypsin:_________ Trypsin:_________ Elastase:_________ 1. SR−SG 2. SF−SG 3. SK−SG 4. SA−SG 5. SV−SG 6. SM−SG

I need help with this question. I have an exam in biological chemistery this month, so I try to be prepared. This is an exam question from last year, that I'm trying to figure out how to calculate WITHOUT using computer (its not allowed during exam).  I will appreciate details when explaining this exercise, so I can understand it. Thank you.

Physiology Michaelis Menten relations

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Part 1: Assess the following partial results section below by editing it for brevity by omitting any unnecessary parts (1 point), explain why you decided to remove certain sections (1 point): To evaluate inhibitory effects of the selected molecules, 10mM stock solutions of each molecule were prepared in DMSO. A reaction mixture (200μl) was prepared with the same formula optimized for the enzyme activity assay (0.1 M Tris-HCl ph 8, 0.1 M KCI, 25 mM NaCl, 0.25 mM ATP, and two units of inorganic yeast pyrophosphatase) with 10 µM of the sample molecule. The reaction mixture was incubated for 20 minutes at ambient temperature. Enzymatic reaction was triggered by addition of the substrate B (0.2 mM) and the absorbance of the product was monitored at 290 nm for 10 minutes. Six out of 15 sample molecules showed appreciable inhibition at 10 μM (Figure 5). Three of the molecules, A3, A6, and A7 exhibited more than 50% inhibition of the enzyme activity and were further diluted to find the minimal…

1 pt pt 9146 Bb 9146 Bb 1031 Class Etsy E Traps E Traps New Free Chat + ☆ 出口 keAssignment/takeCovalentActivity.do?locator-assignment-take [References] You do an enzyme kinetic experiment and calculate a Vmax of 118 μmol per minute. If each assay used 0.10 mL of an enzyme solution that had a concentration of 0.20 mg/mL, what would be the turnover number if the enzyme had a molecular weight of 128,000 g/mol? (Enter your answer to two significant figures.) turnover number = sec-1 D 1 pt Submit Answer Try Another Version 2 item attempts remaining estion stion 5 on 6 7 1pt 1 pt 1 pt 1pt 1pt 1pt 1 pt 1 pt D is the substrate concentration multiplied by the catalytic constant. KM is equivalent to the substrate concentration multiplied by the ratio of rate constants for the formation and dissociation of the enzyme-substrate complex. KM is equivalent to the substrate concentration. KM is equivalent to the substrate concentration divided by 2 A: KM is equivalent to the substrate concentration…

Lineweaver-Burk plots of enzyme kinetics for the reaction, S <-> P, has the following features: 1/v is zero when 1/[S] equals -40 liter mole^-1; 1/[S] is zero when 1/v equals 2.0 x 10^5 min mole^-1. What are the Vmax and Km?

This question should be answered with two or three sentences using relevant biochemical vocabulary.

Question:: Acyl CoA synthetase hydrolyzes ATP to AMP + PPI (pyrophosphate) as part of the activation of fatty acids to fatty acyl-CoA. Explain the role played by the enzyme inorganic pyrophosphatase in this reaction (in the activation of fatty acids to fatty acyl CoA) in the space provided below.

Please help me and explain question 1)

Lineweaver-Burk plots of enzyme kinetics for the reaction, S <-> P, has the following features: 1/v is zero when 1/[S] equals -40 liter mole^-1; 1/[S] is zero when 1/v equals 2.0 x 10^5 min mole^-1. What are the Vmax and Km? Vmax = 5 umol min^-1, Km = 2.5 mM? Vmax = 5 mmol min^-1, Km = 25 M? Vmax = 5 umol min^-1, Km = 25 mM? Vmax = 5 mol min^-1, Km = 2.5 mM? Vmax = 5 mol min^-1, Km = 25 mM?