Question

The melting point, is propor- tional to the number of hydrogen bonds Which one has the most (highest melting point) versas the least. In one plot, draw melting curves for two double strand DNA molecules A and B. Both DNA molecules have the same length of 1000 base pairs. Which DNA duplex has higher melting point and why? DNA molecule A is formed by poly A and poly U strands. DNA molecule B is formed by poly G and poly C strands. Plugin values Myoglobin isolated from alligator's muscle is a monomeric protein. It has 3 time stronger affinity for oxygen than human myoglobin with p50 = 1.8 Torr. 1) (Plug in values) make a plot of alligator myoglobin oxygen saturation (Y) as a function of oxygen pressure. (Hint: use pressure values from 0 Torr to 20 Torr and equation Y = pO2/(po2+p50), 2) At what oxygen pressure is the fractional saturation 75 %. → Find to find the pU2 For my valve oY is. 75 OY 75% 3 in Hinestly you would also expect a two Fold decrease In human hemoglobin, distal histidine residues were mutated to leucine, resulting to a two fold decrease in oxygen affinity The 1053 Wanity means the communicat.on a) Do you expect a cooperative oxygen binding? Explain your reasoning. ok topeshurly will also be neyahuely affected created to the b) The wild type hemoglobin has p50 = 26 Torr. What is p50 value for mutated hemoglobin. only for oxygen. c) Draw an oxygen binding curve for wild type hemoglobin with p50 = 26 and Torr and for mutated hemoglobin (Hint: You do not have to perform calculation as in Problem 2, just draw the expected curve. Wild type cuyes regular cooperatwe one, while for the mutant anticipate one similar to myglobin You have a 2.0 mL sample of myoglobin that shows an absorbance at 555 nm of 1.2. The extinction coefficient of myoglobin is 12.9 mm 4 cm-?. The optical path is 1 cm. Molecular mass:1 17.6 kDa). a) Determine the number of molecule of myoglobin in your sample. -> A=eCL Beer's Law b) How many grams of iron is in your sample? 2 Volane to find moles from the calculated concentration Avogadros number for molecules. Kelationship of UOM! iyon to moles of myoglobin to get grams of

Answer 1

(3 al coopercebinity bennees herman hemoglobin deereases if histidine u replaced by lealline as histidine doRinot ateb allow othy substa to bind at home position. (b) of wild to be po = 26 Torg than offer replacing this with her oxfyon bindin affinity will also decrease 2fold, ie por el 18 for is. Po for muitted hemoglobin will increase PC2) = 262624 2toor (Show low affinity I normal/wild hemoglotain (Oso = 26) 102 47 753, + mutated hemoglobin (Oso=42) 2597 A 12.9 X1 Po (Tor gla A - ExcXL 2 1.2 - 129 X CX 7 > C>(1:2 ) - 0.098 mm > Ma met w y ) 0.093 - Gram kong x2) x 100 morreular 17 x V/96X/03 X 2- = -(0.093 X 1146X103x2) = 21873-6 m myglohn, So, we know that, mal lot of Hengen cosstais Avogadrone. 117.64103 - 6.023x10 23 molence 21878.6 (6.023x10 23 x 21873.6) . 112.6x103 - 1.12 x 1023 miloule 16 I say gobon moteule have a molecule of Iron 1176403 Dating mygobin 42google 0.0Bom my myoglobin = 0.093 mon girm 0.093x20= w.jioning moy.wzgironi M. ml) - 0.093 x 42x2 = test. of imings 7 7.812 gm of iron

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