Topic 7. Acids, Bases, Buffers, Titrations, Polyprotic acids
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1 Topic 7 cids, Bses, Buffers, Titrtions, Polyprotic cids
2 Conjugte cids & bses
3 Strengths of cids & bses strong cid or strong bse is completely dissocited in queous solution. Wek cids nd Wek Bses
4 Crboxylic cids re Wek cids nd mines re Wek Bses sk yourself
5 Buffers Buffered solution resists chnges in p when smll mounts of cids or bse re dded or when dilution occurs. p dependence of the rte of prticulr enzyme-ctlyzed rection. The rte ner p 8 is twice s the rte t p 7 or 9
6 The enderson-sselblch eqn logk (q) pk p log p p pk (q) log log pk log (q) bse cid when K -
7 If p = pk, [] = [ - ] If p < pk, [] > [ - ] If p > pk, [] < [ - ] [ - ] / [] p 100:1 pk + 10:1 pk + 1 1:1 pk 1:10 pk -1 1:100 pk -
8 Prepring Buffer in Rel Life Suppose you wish to prepre 1.00 L of buffer contining M tris t p When we sy M tris, we men tht the totl concentrtion of tris plus tris + will be 0.100M. 1. Weigh out mol tris hydrochloride nd dissolve it in beker contining bout 800 ml wter nd stirring br.. Plce p electrode in the solution nd monitor the p. 3. dd NO solution until the p is exctly The electrode does not respond instntly. 4. Trnsfer the solution to volumetric flsk nd wsh the beker nd stirring br few times. dd the wshings to the volumetric flsk. 5. Dilute to the mrk nd mix.
9 Buffer cpcity Buffer cpcity mesures how well solution resists chnges in p when cid or bse is dded. The greter the buffer cpcity, the less the p chnges. The mount of + or O - tht buffered solution cn bsorb without significnt chnge in p
10 Buffer cpcity ) Mgnitudes of [] nd [ - ] the cpcity of buffered soln. Ex : soln : 5.00 M Oc M NOc soln B : 0.05 M Oc M NOc : p chnge when 0.01 mol of Cl(g) is dded mol B : mol
11 Buffer cpcity 3) [ - ] / [] rtio the p of buffered soln. C : % mol originl soln mol 50.5% new soln 49.5
12 ow indictors work 1) Usully wek orgnic cid or bse tht hs distinctly different colors in its nonionized & ionized forms. In (q) + (q) + In- (q) nonionized ionized form form pk In
13 ow indictors work ) In In 10 show the color of p pk In -1 In In In 10 show the color of p pk In 1 In - In In combintion of the color of In & In -
14 ow indictors work 3) The useful p rnge for indictor is pk In ± 1 encompss the p t equivlence point of titrtion curve 4) Not ll indictors chnge color t the sme p.
15
16 cid-bse Titrtions 1) Strong bse + Strong cid 3 regions : ) excess bse b) equivlence point (p = 7.00) c) excess cid
17 ) Wek cid + Strong bse 4 regions: ) excess wek cid b) buffer region c) equivlence point (p > 7.0) d) excess bse
18 3) Wek bse + Strong cid 4 regions: ) excess wek bse b) buffer region c) equivlence point (p < 7.00) d) excess cid
19 b) Using p Electrode to Find the End Point using titrtion curve
20 Prcticl Notes Primry stndrds: cids nd bses cn be purchsed in forms pure enough. NO, KO must be stndrdized ginst primry stndrd lkline solutions: (ex: NO) O - + CO CO 3 - Strong bse ttcks glss.
21 Prcticl Notes
22 Typicl pplictions of neutrliztion titrtions : Kjeldhl Nitrogen nlysis Developed in 1883, the nlysis remins one of the most widely used methods for determining nitrogen in orgnic substnces such s protein, cerel, nd flour. The solid is digested (decomposed nd dissolved) in boiling sulfuric cid to convert nitrogen into mmonium ion, N 4+, in long-neck Kjeldhl flsk
23 Melmine contminted milk
24 Kjeldhl Nitrogen nlysis: Chemistry Melmine (66.6wt% nitrogen) Behind the elth Cynuric cid (3.6 wt% N) Protein source Met Blood plsm Milk Flour Egg Weight% nitrogen
25 Polyprotic cids nd Bses
26 mino cids re polyprotic mino cids from which proteins re built hve n cidic crboxylic cid group, bsic mino group, nd vrible substituent designted R: The resulting structure, with positive nd negtive sites, is clled zwitterion.
27 mino cids re polyprotic
28
29 Finding the p 1) Titrtion of polyprotic cids (ex) 3 PO 4 ( 3 ) p p pk pk 1 p pk [ [ ] ] [ 50% 50% 100% ] p pk % [3] [ 50% 50% ] V of NO
30 Finding the p ) solutions contining mphoteric nions ( - ) s the only -B mjor species (q) (q) 3 (q) (q) 3 K - 3 K K 1
31 Finding the p.. K K K from K K K (q)
32 Finding the p & pk pk p K K K K K
33 Which is the principle species? 1). p pk log t p 4.0 p pk p pk 1
34 Which is the principle species? ) For p pk 1 p 1 (pk 1 pk ) p pk
35 3) For 3
36 Ex Wht is the principl form of rginine t p 10.0? pproximtely wht frction is in this form? Wht is the second most bundnt form t this p?
37 Proteins re polyprotic cids nd bses myoglobin
38 Titrtions in Polyprotic Systems Isoelectric p (isoionic p) The p t which the verge chrge of the polyprotic cid is zero
39 Titrtions in Polyprotic Systems (ex) C 3 C N CCOO 3 + N C lnine ction + COO pk 1 =.35 C 3 C N CCO N CCO - - lnine ntion + + pk =9.87 isoelectric p : most form s where p 1 pk 1 pk &
40 Titrtions in Polyprotic Systems Isoelectric focusing : technique of protein seprtion p grdient design Protein stop migrting in n electric field t isoelectric p
41 omework 1. Drw the structures of the predominnt forms of glutmine cid nd tyrosine t p 9.0 nd p Wht is the second most bundnt species t ech p?. Clculte the p of 0.10M solution of ech of the following mino cids in the form drwn:
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