The absorption spectra for three different amino acids, phenylalanine (Phe), tryptophan (Trp), and tyrosine (Tyr) are shown at right. The plot is the molar & absorptivity & versus wavelength. Order the three amino acids according to their ability to absorb 210 nm light when all three are at equimolar concentrations. 40,000 20,000 10,000 5,000 2,000 1,000 500 200 100 50 20 10 |||||||| 200 220 Phe 240 260 λ (nm) Trp Tyr 280 300 320
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The answer choices are highest, lowest, and intermediate absorption.
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- Describe the structuraldifferences betweenthe oxidized form andthe reduced form ofnicotinamidec reaction of okt ndar vulaln i formation of substances. ng diethyl ether from ethanol at STP, using the value al ial effect (Qre the ren 44150HM LEAmhnat** S .. using the a rage values of theiuIdard enthalny or is 54 g. 3. In 100 g of cod on average contains 11.6 g of protein and 0.3 g of fat. Calculate (in kJ and kcal) the energy that will be released during the assimilation of a portion of cod weighing 228 g. amhustin i the mass of 4. In the human body ethanol is oxidized in two atoThis is a visible spectra between 390-590 nm obtained during the protein separation process of haemoglobin and cytochrome c using CM Sephadex chromatography. I'd like the results shown on the image interpreted. Look for characteristic peaks or patterns that correspond to the absorption properties of these proteins in the visible range.
- Phospholipases show an enhanced activity for a substrateabove the critical micelle concentration. (The critical micelleconcentration, or cmc, is that concentration of a lipid abovewhich micelles begin to form.)a. What type of noncovalent interactions are possiblebetween the lipid and the enzyme at this stage?b. What do these interactions suggest about the structure ofphospholipases?1. The amino acid sequence for the protein lysozyme is given below. Estimate the isoelectric point for lysozyme protein. The pK, values are provided in Table 3.1. KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNT DGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKK IVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL Here's the sequence in this form: LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS ARG HIS GLY Table 3.1 Typical pk, values of ionizable groups in proteins Group Acid Typical pK, Base Terminal a-carboxyl 3.1 group Aspartic acid Glutamic acid 4.1 N. Histidine 6.0 -N + H Terminal a-amino group 8.0 Cysteine 8.3 Тутosine 10.9 + H Lysine 10.8 H H. + N-H Arginine 12.5 N-H N-H Note: Values of pk, depend on temperature, ionic strength, and the microenvironment of the ionizable group. inThereareseveralwaystoproducetheaminoacidsthatbuildaprotein.What does this mean?
- Give two benefits of utilizing the biuret reaction to assess protein concentration over directly measuring protein absorbance at 280 nm.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) 0.41whats the amino acid squence for this
- Give two advantages and two disadvantages to using the biuret reaction to measure protein concentration compared to measuring the protein absorbance directly at 280 nmThe interconverison of DHAP and GAP greatly favors the formation of DHAP at equilibirum. Yet the conversion of DHAP by triose phosphate isomerase proceeds readily. Why?The enzyme serine hydroxymethy ltransferase (SHMT) catalyses the conversion of serine into glycine. The fo llowing table gives the initial rates, vo, for the SHMT-catalysed reaction of the substrate serine at var ious concentratio ns of serine, lSI.[S]/(mmol dm-3) 10 20 30 40vo(μmol dm-3 s-1) 1.63 2.94 4.10 4.95Use the data to determine the values of the MichaelisMenten constant, the maximum velocity of the reaction, and the maximum turnover number of the enzyme.