300.0 mg conc 0.100 M expID: HM1-001 scale 1) EDCI, HOBT hydrate DIPEA O`HN NH H3CO HN DCM:DMF (1:2) NH 2) workup with 1M HCI (aq.) (add first for 10 min (add second after pre-activation) pre-activation) Boc-Asp(OMe)-OH•DCHA H-Phe-OtBu•HCI Boc-Asp(OMe)-Phe-OtBu molar MW m d V
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- Calculate delt G for a.) CH3NH2(aq) + H2O (l) -> CH3NH3+ (aq) + OH-(aq) T= 25C kp= 4.4x 10-4 b.) Pbl2(s) + Pb2+(aq) +2I-(aq) T= 25C Kp= 8.7x10-9The measurement of LDH in the serum can be used to diagnose whether tissue damage hasoccurred.Students were tasked with the development of an assay for LDH activity in human serum samplesfrom a control patient (healthy) and a patient who had suffered cardiac damage. Two samples wereprovided, labelled C and D (Control and Diseased serum).The students decided to follow the loss of absorbance of NADH in an appropriate assay buffercontaining pyruvate as the substrate. Q1 (a) By examining the absorbance spectra(in the image attached) of both NAD+ and NADH below, comment why this approach is suitable strategy. Q1 (b). What would be the optimum wavelength at which they should measure absorbance? Give a reason for your answer. The students conducted the assay for LDH activity using the two serum samples. Each cuvette (path length 1 cm) contained 3ml of a suitable assay buffer (including pyruvate as substrate). 20 microlitres of either serum was added to the cuvette and the absorbance values…How can I isolate mJuce in the equation, Please go step by step mJuce * XJuce = (mJuce-mVapor) *XConcentrate
- 1. H2O; 2. KMnO4 1. O3; 2. DMS; 3. Na2Cr2O7/H2SO4/H2O 1. NaOH, Br2; 2. DMS; 3. H2O/heat 1. O3; 2. DMS; 3. KMnO4 1. DMS; 2. H2O/heatGiven this reaction: ZNG) + 2HCI @q3 Hz (qD +Zn Cl2(aq) a) Descrive Hhe effect of increasing the cancentratian ag on the readtich rate cund response in terms of collisian theory |cdenti fy ane other Variable Hhat mignt affect fhe rate cand shoud be held constent dur ing this inestigation the wckependent and dependent vasi abre Of HCl jasti fy your c) ldentiey in this Thiestigation/Isl.exe/lo_u-IgNSIkr7j8P3jH-IQs_dp5pR4ENzvdYC-70kXyMz36Bqhw3sVPj_jpaFLxvGArYxlbmcyqa71YYPJBG6RjdYAdGPjGhFLILID-HEX1YcqAB?1oBw7QYjlbavbSPXtx-YCjsh_7mMmrq#3 P Course Home Login | Student Veri... Bb Logout MyProgrammingLab Imported From IE ITEC2110:Summer2... TunesToTube - Upl.. Web Development.. Pub O KINETICS AND EQUILIBRIUM Using a second-order integrated rate law to find concentration c.. Consider this reaction: 2HI (g) → H, (g) +I, (g) At a certain temperature it obeys this rate law. rate = (0.118 M-s)[H] ? Suppose a vessel contains HI at a concentration of 1.48 M. Calculate the concentration of HI in the vessel 42.0 seconds later. You may assume no other reaction is important. Round your answer to 2 significant digits. x10 II
- met (b) Find the forward (k, Jand reverse (k-) rate constants for the recombination kuk-s reaction; OH +H* H20 at 25 °C, 40)-0.51 x 1016 M1 Given: K, = LHOM.H)text Nu Whe ofect wokl hgh presure have on the proketon of NOg? Why? 4 Wharwoud be the efat of ach of the fulowing on the equilbrium iimvolving the reacion o coke (C (s) when e prokre CO and H C) H,0) cog)+ H,(E) Akten of steam An increase in pvessure Removal of H as it is prodced Akng a catalst S he birding of axygen to hemagbbin (abbreviated Hb). giving oxyhemogldbin (HbO,) s partially glaed by he compk ad tcan be summarized as bolows: contraon of H and CO, in the blood. Although the equilibrum is very HbO, H CO, co,HbH + o, Accordg to Le Chaelers Princpe what wauld be the effect of each of the following on the squban? a The produc on of ac acid (whch contairs Hr) and CO, in a muscle during vigorous exercise? ng besh oxygen aiched a?For an enzyme -catalyzed reaction, KM=10.0 mmol dm-3, vmax=0.250 mmol dm²³ s-'; [E]o= 2.3 x 10-6 mmol dm-3. Calculate the catalytic efficiency (=kb/KM) of the enzyme. 0.920 dm³ mol-l s-1 3.1 x 107 dm³ mol-1 s-1 1.1 x107 dm³ mol-l s-1 0.250 dm³ mol-l s-1
- H3O* (aq) + OAC° (aq) Н2о () + НОАc (аq) +» НҙО* (аq) + ОАc" (аq) the Dissociation Constant Ka of HOAC: Ka = [HOAC]/([H30*][OAC¯]) Ka = [H3O*][OAc]/([HOAC][H2O]) Ka = [H3O*][OAc"]/[HOAC] O Ka = [HOAC][H2O]/([H3O*][OAC¯]) %3DReaction Velocity (mm/sec) Ma no !! L [1 1 L IM 3M FO Substrate Concentration (M) 1. IN Which statement is true? KM AN ALM 4V The graph above displays the kinetic profiles of the same enzyme catalyzing two different substrates. The red curve displays the higher turnover number (kcat). The red curve displays higher affinity between substrate and enzyme. The blue curve displays competitive inhibition. The red curve displays higher cooperativity,a) A heduogencom renetant catalyst warki by intee aitling buailing called adiorption - loith in process dury this piees ? axplain ohat ocuus how this lower the acti vation Can ut deu increase the area what hetuo genea. have catalyel On the sufau incuring activation Enugy? axplain yau auee Dou preaction ? awwe. Hect the