CHAPTER 2

CHEMICAL COMPONENTS OF CELLS

2004 Garland Science Publishin
Che!ical "#nds
2-1 If the isotope
32
S has 16 protons and 16 neutrons, how many protons and how many
neutrons will the isotope
35
S have?
2-2 A. If 0.5 mole of lu!ose weihs "0 , what is the mole!ular weiht of lu!ose?
#. $hat is the !on!entration, in rams per liter %&l', of a 0.25 ( solution of
lu!ose?
). *ow many mole!ules are there in 1 mole of lu!ose?
2-3 $hi!h of the followin elements is +,AS- a.undant in livin oranisms?
%a' Sulfur
%.' )ar.on
%!' /0yen
%d' 1itroen
%e' *ydroen
2-4 2our friend learns a.out Avoadro3s num.er and thin4s it is so hue that there may not
even .e a mole of livin !ells on ,arth. 2ou have re!ently heard that there are a.out 50
trillion %50 10
12
' human !ells in ea!h adult human .ody, so you .et your friend 55 that
there is more than a mole of !ells on ,arth. /n!e you learn that ea!h human !ontains
more .a!terial !ells %in the diestive system' than human !ells, you are sure that you have
won the .et. -he human population is now more than 6 .illion %6 10
"
'. $hat
!al!ulation !an you show your friend to !onvin!e him you are riht?
2-5 Atoms form !ovalent .onds with ea!h other .y
%a' sharin protons.
%.' sharin ele!trons.
%!' transferrin ele!trons from one atom to the other.
%d' sharin neutrons.
%e' attra!tion of positive and neative !hares.
2-6 A !ar.on atom !ontains si0 protons and si0 neutrons.
A. $hat are its atomi! num.er and atomi! weiht?
#. *ow many ele!trons does it have?
). $hat is its valen!e? *ow does this affe!t !ar.on3s !hemi!al .ehavior?
6. )ar.on with an atomi! weiht of 17 is radioa!tive. *ow does it differ in stru!ture
from nonradioa!tive !ar.on? *ow does this differen!e affe!t its !hemi!al
.ehavior?
$%
2-7 An ioni! .ond .etween two atoms is formed as a result of the
%a' sharin of ele!trons.
%.' loss of a neutron from one atom.
%!' loss of ele!trons from .oth atoms.
%d' loss of a proton from one atom.
%e' transfer of ele!trons from one atom to the other.
2-8 $hi!h of the followin pairs of elements are li4ely to form ioni! .onds? 8se 9iure :2;<
if ne!essary.
9iure :2;<
%a' *ydroen and hydroen
%.' (anesium and !hlorine
%!' )ar.on and o0yen
%d' Sulfur and hydroen
%e' )ar.on and !hlorine
$4
2-9 9or ea!h of the followin senten!es, fill in the .lan4s with the .est word or phrase
sele!ted from the list .elow. 1ot all words or phrases will .e used= ea!h word or phrase
should .e used only on!e.
$hereas ioni! .onds form a%n' >>>>>>>>>>>>>>>>>>, !ovalent .onds
.etween atoms form a%n' >>>>>>>>>>>>>>>>>>. -hese !ovalent .onds
have a !hara!teristi! .ond >>>>>>>>>>>>>>>>>> and .e!ome stroner and
more riid when two ele!trons are shared in a%n' >>>>>>>>>>>>>>>>>>.
,?ual sharin of ele!trons yields a%n' >>>>>>>>>>>>>>>>>> !ovalent
.ond. If one atom parti!ipatin in the .ond has a stroner affinity for the
ele!tron, this produ!es a partial neative !hare on one atom and a partial
positive !hare on the other. -hese >>>>>>>>>>>>>>>>>> !ovalent .onds
should not .e !onfused with the wea4er >>>>>>>>>>>>>>>>>> .onds that
are !riti!al for the three;dimensional stru!ture of .ioloi!al mole!ules and
for intera!tions .etween these mole!ules.
!hare lenth polar
!ovalent mole!ule salt
dou.le .ond non!ovalent sinle .ond
ioni! nonpolar weiht
2-10 A. In what s!ientifi! units is the strenth of a !hemi!al .ond usually e0pressed?
#. If 0.5 4ilo!alories of enery is re?uired to .rea4 6 10
23
.onds of a parti!ular
type, what is the strenth of this .ond?
2-11 Appro0imately how many hydroen .onds does it ta4e to ive an areate .indin
strenth nearly e?ual to a sinle !ovalent .ond?
%a' 1
%.' 3
%!' 50
%d' 500
%e' 5000
2-12 After loo4in at 9iure :2;< a.ove, whi!h of the followin pairs of atoms do you e0pe!t
to .e a.le to form dou.le .onds with ea!h other?
%a' ( and )a
%.' ) and )l
%!' S and /
%d' ) and *
%e' *e and /
$&
2-13 A. S4et!h three different ways three water mole!ules !ould .e held toether .y
hydroen .ondin.
#. /n a s4et!h of a sinle water mole!ule, indi!ate the distri.ution of positive and
neative !hare %usin the sym.ols
@
and
A
'.
). *ow many hydroen .onds !an a hydroen atom in a water mole!ule form? *ow
many hydroen .onds !an the o0yen atom in a water mole!ule form?
2-14 $hi!h of the followin statements a.out hydroen .onds are -B8,?
%a' -hey are wea4 !ovalent .onds that are easily disrupted .y heat.
%.' -hey are wea4 .onds formed .etween hydro!ar.ons in water.
%!' -hey are wea4 .onds formed .etween nonpolar roups.
%d' -hey are wea4 .onds only formed in the presen!e of water.
%e' -hey are wea4 .onds involved in maintainin the !onformation of
ma!romole!ules.
2-15 #ased on what you 4now a.out the properties of water, whi!h of the followin statements
a.out methanol %)*
3
/*' are -B8,?
%a' (ethanol mole!ules form more hydroen .onds than water mole!ules do.
%.' -he .oilin point of methanol is hiher than that of water.
%!' Salts su!h as 1a)l are less solu.le in methanol than in water.
%d' (ethanol is a more !ohesive li?uid than water.
%e' (ethanol has a hiher surfa!e tension than water.
2-16 A. $hat is the p* of pure water?
#. $hat !on!entration of hydronium ions does a solution of p* < !ontain?
). )omplete the followin rea!tionC
)*
3
)//* @ *
2
/
6. $ill the rea!tion in ) o!!ur more readily %.e driven to the riht' if the p* of the
solution is hih?
$'
2-17 -he amino a!id histidine is often found in enDymes. 6ependin on the p* of its
environment, sometimes histidine is neutral and other times it a!?uires a proton to
.e!ome positively !hared. )onsider an enDyme with a histidine side !hain that is 4nown
to play an important role in the fun!tion of the enDyme. It is not !lear whether this
histidine is re?uired in its protonated or unprotonated state. -o answer this ?uestion you
measure enDyme a!tivity over a rane of p*, with the results shown in 9iure :2;1E.
$hi!h form of histidine is ne!essary for the a!tive enDyme?
9iure :2;1E
M#lecules in Cells
2-18 (at!h the !hemi!al roups shown in the first list with their names sele!ted from the
se!ond list.
List 1 List 2
A. A/* 1. Amino
#. A) F / 2. Aldehyde
). A)//* 3. Ghosphate
6. A)*
3
7. )ar.o0yl
,. A1*
2
5. )ar.onyl %4etone'
6. (ethyl
E. Amido
<. ,ster
". *ydro0yl
$(
2-19 (at!h the ma!romole!ules shown in the first list with their small mole!ule .uildin
.lo!4s from the se!ond list.
List 1 List 2
A. Golysa!!harides 1. Amino a!ids
#. 61A 2. 6eo0yri.onu!leotides
). B1A 3. Aldehydes
6. Groteins 7. Gyrophosphates
,. +ipids 5. Bi.onu!leotides
6. 9atty a!ids
E. Suars
<. Steroids
2-20 $hi!h of the followin are e0amples of isomers?
%a'
17
) and
12
)
%.' Alanine and ly!ine
%!' Adenine and uanine
%d' Hly!oen and !ellulose
%e' Hlu!ose and ala!tose
2-21 $hi!h of the followin is 9A+S, of !ondensation rea!tions?
%a' Grodu!e many .ioloi!al polymers from monomers.
%.' )onsume *
2
/ mole!ules.
%!' Aid in storae of enery reserves.
%d' Are the opposite of hydrolysis rea!tions.
%e' Are usually !atalyDed in !ells .y enDymes.
2-22 A. *ow many !ar.on atoms does the mole!ule represented in 9iure :2;22 have?
#. *ow many hydroen atoms?
). $hat type of mole!ule is it?
9iure :2;22
$)
2-23 /n the phospholipid mole!ule in 9iure :2;23 la.el ea!h num.ered line with a !orre!t
term sele!ted from the list .elow.
A. Ghosphate
#. 1onpolar head roup
). Hly!erol
6. Golar head roup
,. Saturated fatty a!id
9. A!eti! a!id
H. Suar
*. *ydropho.i! reion
I. *ydrophili! reion
I. 1onsaturated fatty a!id
9iure :2;23
2-24 Ghospholipids !an form .ilayer mem.ranes .e!ause they are
%a' hydropho.i!.
%.' lipids.
%!' amphipathi!.
%d' hydrophili!.
%e' amphoteri!.
2-25 A. $rite out the se?uen!e of amino a!ids in the followin peptide usin the
full names of the amino a!ids.
GroAJalA-hrAHlyA+ysA)ysAHlu
#. $rite the same se?uen!e usin the sinle letter !ode for amino a!ids.
). A!!ordin to the !onventional way of writin the se?uen!e of a peptide or a
protein, whi!h is the );terminal amino a!id and whi!h is the 1;terminal amino
a!id in the a.ove peptide?
$*
2-26 $hi!h of the followin statements a.out amino a!ids is -B8,?
%a' -wenty;two amino a!ids are !ommonly found in proteins.
%.' (ost of the amino a!ids used in protein .iosynthesis have !hared side !hains.
%!' Amino a!ids are often lin4ed toether to form .ran!hed polymers.
%d' 6; and +;amino a!ids are found in proteins.
%e' All amino a!ids !ontain an 1*
2
and a )//* roup.
2-27 Groteins !an .e modified .y a rea!tion with a!etate that results in the addition of an a!etyl
roup to lysine side !hains as shown in 9iure :2;2E. -he .ond shown in the .o0 in the
a!etylated lysine side !hain is most li4e a%n'
9iure :2;2E
%a' ester.
%.' peptide .ond.
%!' phosphoanhydride .ond.
%d' hydroen .ond.
%f' phosphoester .ond.
2-28 61A differs from B1A in
%a' the num.er of different .ases used.
%.' the num.er of phosphates .etween the suars in the suar;phosphate .a!4.one.
%!' the 4ind of suar found in the suar;phosphate .a!4.one.
%d' one of the purines used.
%e' the !hemi!al polarity of the polynu!leotide !hain.
2-29 $hi!h of the followin statements is 9A+S, a.out A-G?
%a' )ontains hih enery phosphoanhydride .onds.
%.' Is sometimes !alled the Kuniversal !urren!yL in the enery e!onomy of !ells.
%!' )an .e in!orporated into 61A.
%d' )an .e hydrolyDed to release enery to power hundreds of rea!tions in !ells.
%e' )omprises a suar, phosphate roups, and a nitroenous .ase.
20
2-30 $hi!h of the followin are li4ely to .e disrupted .y hih !on!entrations of salt?
%a' A lipid .ilayer
%.' -he peptide .onds in a protein
%!' A !omple0 of two proteins
%d' -he suar;phosphate .a!4.one of a nu!lei! a!id
%e' An oil droplet in water
Macr#!#lecules in Cells
2-31 2ou are tryin to ma4e a syntheti! !opy of a parti!ular protein .ut a!!identally Moin the
amino a!ids toether in e0a!tly the reverse order. /ne of your !lassmates says the two
proteins must .e identi!al, and .ets you 520 that your syntheti! protein will have e0a!tly
the same .ioloi!al a!tivity as the oriinal. After havin read this !hapter, you have no
hesitation in sta4in your 520 that it won3t. $hat parti!ular feature of a polypeptide !hain
ma4es you sure your 520 is safe, .ut that your proMe!t will have to .e redone.
2-32 A protein !hain folds into its sta.le and uni?ue 3;6 stru!ture, or !onformation, .y ma4in
many non!ovalent .onds .etween different parts of the !hain. Su!h non!ovalent .onds
are also !riti!al for intera!tions with other proteins and !ellular mole!ules. 9rom the list
provided, !hoose the !lass%es' of amino a!ids that are most important for the intera!tions
detailed .elow.
A. 9ormin ioni! .onds with neatively !hared 61A
#. 9ormin hydroen .onds to aid solu.ility in water
). #indin to another water;solu.le protein
6. +o!aliDin an Kinteral mem.raneL protein that spans a lipid .ilayer
,. Ga!4in tihtly the hydropho.i! interior !ore of a lo.ular protein
a!idi! nonpolar
.asi! un!hared polar
2-33 61A is neatively !hared at physioloi!al p*. A protein N .inds to 61A throuh
non!ovalent ioni! intera!tions involvin lysines. $hat will .e the effe!t of a!etylation of
the lysine side !hains %see 9iure :2;2E' in protein N on the strenth of this .indin?
%a' It should in!rease .e!ause the a!etylated lysine will form a reater num.er of
ioni! intera!tions with 61A.
%.' It should de!rease .e!ause the a!etylated lysine no loner has a positive !hare.
%!' It should have no effe!t .e!ause the unmodified lysine would not have formed an
ioni! intera!tion with the 61A.
%d' It should have no effe!t .e!ause the .ond formed .etween lysine and the a!etyl
roup still has a positive !hare.
%e' It should de!rease unless the 61A !an .e!ome more neatively !hared.
2$
2-34 2ou are studyin a mi!rooranism in whi!h a KmaleL turns pin4 in the presen!e of a
Kfemale.L -he male .e!omes pin4 .e!ause a protein O se!reted .y the female .inds to
and a!tivates a protein 2 on the male that is responsi.le for the !olor !hane. 2ou have
isolated a strain of the mi!rooranism that produ!es a mutant form of protein O. -his
strain .ehaves normally at temperatures lower than 3E), .ut at hiher temperatures it
!annot turn pin4. )ould any of the followin !hanes in mutant protein O e0plain your
results? If so, whi!h ones, and e0plain why.
%a' It ma4es an e0tra hydroen .ond to protein 2.
%.' It ma4es fewer hydroen .onds to protein 2.
%!' It ma4es a !ovalent .ond to protein 2.
%d' It is !ompletely unfolded at temperatures lower than 3E).
%e' It is !ompletely unfolded at temperatures hiher than 3E).
%f' It is una.le to .ind to protein 2 at any temperature.
22
Ans+ers
2-1 16 proteins and 1" neutrons
2-2 A. 1<0 daltons. A mole of a su.stan!e has a mass e?uivalent to its mole!ular weiht
e0pressed in rams.
#. 75 &l
). 6 10
23
mole!ules
2-3 %a' Sulfur is the least a.undant element amon the !hoi!es iven.
2-4 Avoadro3s num.er, or 6 10
23
, is the num.er of atoms %or units' in a mole. If you
multiply the num.er of people on ,arth .y the num.er of !ells in the human .ody, then
dou.le it to a!!ount for the .a!teria, you will !al!ulateC %6 10
"
' %50 10
12
' 2 F 6
10
23
. -hus, there must .e mu!h more than a mole of livin !ells on ,arth, and you win
55.
2-5 %.'
2-6 A. -he atomi! num.er of !ar.on, whi!h is the num.er of protons, is si0. -he atomi!
weiht, whi!h is the num.er of protons plus neutrons, is 12.
#. -he num.er of ele!trons, whi!h e?uals the num.er of protons, is si0.
). -he valen!e is the minimum num.er of ele!trons that must .e lost or ained to fill
the outer shell of ele!trons. -he first shell !an a!!ommodate two ele!trons and the
se!ond shell, eiht. )ar.on therefore has a valen!e of four .e!ause it needs to
ain four additional ele!trons %or would have to ive up four ele!trons' to o.tain a
full outermost shell. )ar.on is most sta.le when it shares four additional
ele!trons with other atoms %in!ludin other !ar.on atoms' .y formin four
!ovalent .onds.
6. )ar.on17 has two additional neutrons in its nu!leus. As its ele!trons determine
the !hemi!al properties of an atom, !ar.on17 is !hemi!ally identi!al to !ar.on12.
2-7 %e'
2-8 %.' (anesium has a valen!e of two and !hlorine has a valen!e of one. -hus, two
!hlorine atoms !an ea!h a!!ept an ele!tron donated .y manesium to yield a salt,
desinated as ()l
2
that !ontains twi!e as many )l
A
!hlorine anions as (
2@

manesium !ations. All ions in this salt will have full outermost ele!tron shells.
2%
2-9 $hereas ioni! .onds form a salt, !ovalent .onds .etween atoms form a molecule. -hese
!ovalent .onds have a !hara!teristi! .ond length and .e!ome stroner and more riid
when two ele!trons are shared in a double bond. ,?ual sharin of ele!trons yields a
nonpolar !ovalent .ond. If one atom parti!ipatin in the .ond has a stroner affinity for
the ele!tron, this produ!es a partial neative !hare on one atom and a partial positive
!hare on the other. -hese polar !ovalent .onds should not .e !onfused with the wea4er
noncovalent .onds that are !riti!al for the three;dimensional stru!ture of .ioloi!al
mole!ules and for intera!tions .etween these mole!ules.
2-10 A. 4ilo!alories per mole %or 4iloMoules per mole'
#. 0.5 4!al&mole
2-11 %!'
2-12 %!' Sulfur and o0yen .oth re?uire two ele!trons to fill their outer shell and !an do so
.y sharin four ele!trons and formin a dou.le .ond.
2-13 A. See 9iure A2;13A.
#. See 9iure A2;13#.
9iure A2;13
). *ydroen !an form one= o0yen two.
2-14 )hoi!e %e' is the answer. *ydroen .onds are !riti!al for maintainin the !onformation,
or 3;6 stru!ture, of .ioloi!al ma!romole!ules li4e proteins and nu!lei! a!ids. )hoi!e
%a' is false .e!ause hydroen .onds are not !ovalent. )hoi!e %.' is false .e!ause the
nonpolar;)* roups on hydro!ar.ons !annot form ood hydroen .onds, in water or out
of it. )hoi!e %!' is essentially another way of statin !hoi!e %.' and thus is false. )hoi!e
%d' is false .e!ause many mole!ules .esides water !an form hydroen .onds and do so
reardless of whether or not water is present.
24
2-15 )hoi!e %!' is the answer. In methanol one of the hydroens of a water mole!ule has .een
repla!ed .y a nonpolar methyl roup. (ethanol will form fewer hydroen .onds %thus
!hoi!e %a' is false' and ma4e fewer ioni! intera!tions than water does. -he a.ility of
water to dissolve salts is a dire!t !onse?uen!e of its a.ility to ma4e ioni! intera!tions.
Salts are therefore less solu.le in methanol. )hoi!es %.', %d', and %e' are all false .e!ause
the hih .oilin point, hih deree of !ohesion, and hih surfa!e tension of water are all a
result of the e0tensive hydroen .ondin .etween water mole!ules. As methanol ma4es
fewer hydroen .onds, its .oilin point will .e lower, it will .e less !ohesive, and it will
have a lower surfa!e tension than water.
2-16 A. p* E
#. 10
A<
(
). )*
3
)//
A
@ *
3
/
@
6. 2es. If the p* is hih, then the !on!entration of hydronium ions will .e low.
-herefore the rihtward rea!tion, whi!h produ!es hydronium ions, will .e
favored.
2-17 Assumin the !hane in enDyme a!tivity is due to the !hane in the protonation state of
histidine, the enDyme must re?uire histidine in the protonated, !hared state. -he enDyme
is a!tive only at low, a!idi! p*, where the proton %or hydronium ion' !on!entration is
hih and thus loss of a proton from histidine will .e disfavored so that histidine is li4ely
to .e protonated.
2-18 AP"= #P5= )P7= 6P6= ,P1
2-19 APE= #P2= )P5= 6P1= ,P6
2-20 %e' Hlu!ose and ala!tose are .oth si0;!ar.on suars and thus .oth have the formula
)
6
*
12
/
6
. -hey are thus isomers of ea!h other.
17
) and
12
) are e0amples of
isotopes. Adenine and uanine are .ases !ontainin different num.ers of nitroen
and o0yen atoms. Hly!oen and !ellulose are different polymers of lu!ose.
Alanine and ly!ine are amino a!ids with ?uite different side !hains, a methyl
roup and a hydroen atom, respe!tively.
2-21 )hoi!e %.' is the answer. A !ondensation rea!tion releases a water mole!ule when
formin polymers %li4e polysa!!haride enery reserves' from monomeri! units %li4e
simple suars', whereas the reverse hydrolysis rea!tion !onsumes a water mole!ule %thus,
!hoi!es %a', %!', and %d' are !orre!t'. (ost syntheti! rea!tions in !ells are !atalyDed .y
enDymes %thus !hoi!e %e' is !orre!t'.
2&
2-22 A. 20 !ar.on atoms
#. 31 hydroen atoms
). A fatty a!id %9iure A2;22 is an ara!hidoni! a!id'.
9iure A2;22
2-23 1P6= 2PA= 3P)= 7PI= 5PI= 6P*= EP,
2-24 %!'
2-25 A. proline;valine;threonine;ly!ine;lysine;!ysteine;lutami! a!id %or lutamate'
#. GJ-HQ):
). );terminal is lutami! a!id %or lutamate'= 1;terminal is proline.
2-26 )hoi!e %e' is true. As their name implies, all amino a!ids have at lease one amino %1*2'
roup and at least one a!idi! !ar.o0yli! %)//*' roup. It is throuh these two roups
that they form peptide .onds. -here are 20 !ommon amino a!ids %!hoi!e %a' is false', and
four or five of these have !hared side !hains %!hoi!e %.' is false'. ,a!h amino a!id
forms only two !ovalent .onds with other amino a!ids, one .ond at the amino roup and
another at the !ar.o0yl roup %!hoi!e %!' is false'= an e0!eption to this is !ysteine,
.e!ause the side !hains of two !ysteines !an form a !ovalent sulfhydryl .ond to !rosslin4
different reions of a polypeptide !hain. )hoi!e %d' is false .e!ause only +;amino a!ids
are found in proteins.
2-27 %.' -he indi!ated .ond is an amide. +i4e a peptide .ond, it is formed .y rea!tion
.etween a !ar.o0yl roup and an amino roup.
2-28 %!' B1A !ontains the ri.ose suar whereas 61A !ontains the deo0yri.ose suar.
-hey also differ in one of the pyrimidine .ases used= B1A !ontains the
pyrimidine ura!il, while 61A instead !ontains thymine. All the other features are
the same.
2-29 %!' A-G is used in enery !onversions, !ontains ri.ose, and !an .e in!orporated into
B1A. #ut synthesis of 61A re?uires the deo0yri.ose form of the nu!leotide,
dA-G. All the other statements a.out A-G are true.
2-30 )hoi!e %!' is !orre!t. 1on!ovalent ioni! intera!tions su!h as those that hold two proteins
toether are most li4ely to .e disrupted .y salt. +ipid .ilayers %!hoi!e %a'' and a lipid
droplet %!hoi!e %e'' are held toether .y Khydropho.i! intera!tionsL on whi!h salt will
have no effe!t. )hoi!es %.' and %d' are e0amples of !ovalent .onds, whi!h are not
disrupted .y salt.
2'
2-31 As a peptide .ond has a distin!t !hemi!al polarity, a polypeptide !hain also has a distin!t
polarity. %See 9iure A2;31.' -he reversed protein !hains !annot ma4e the same
non!ovalent intera!tions durin foldin and thus will not adopt the same 3;6 stru!ture as
the oriinal protein. -he a!tivities of these two proteins will definitely .e different, sin!e
the a!tivity of a protein depends on its 3;6 stru!ture. It is unli4ely that the reverse !hain
will fold into any well;defined, and hen!e, fun!tionally;useful stru!ture at all, .e!ause it
has not passed the strinent sele!tive pressures imposed durin evolution.
9iure A2;31
2-32 A. .asi!
#. un!hared polar
). un!hared polar, .asi!, and a!idi!
6. nonpolar
,. nonpolar
2-33 )hoi!e %.' is !orre!t. 8nmodified lysine side !hains are positively !hared and hen!e
attra!tive to the neatively !hared 61A %thus !hoi!e %!' is in!orre!t'. #e!ause
a!etylation neutraliDes the positive !hare %thus !hoi!e %d' is in!orre!t', the a!etylated
form of protein N will form fewer ioni! .onds with 61A %thus !hoi!e %a' is in!orre!t',
and thus the strenth of the intera!tion will de!rease. )hoi!e %e' is in!orre!t, sin!e
in!reasin the num.er of neative !hares on 61A would have no effe!t on!e the
positive !hare on the lysine has .een neutraliDed.
2-34 )hoi!es %.' and %e' are possi.le e0planations. If protein O ma4es fewer hydroen .onds
to protein 2, the two proteins will .ind less tihtly and may !ome apart at temperatures
a.ove 3E). -hermal motion is one of the for!es that !an disrupt the wea4 non!ovalent
.onds responsi.le for holdin O and 2 toether. -he male will, therefore, not .e a.le to
turn pin4 a.ove 3E). $ea4 non!ovalent .onds are also responsi.le for foldin O into
the proper 3;6 stru!ture. If protein O is !ompletely unfolded at elevated temperatures it
will not .e a.le to .ind to protein 2, so !hoi!e %e' !ould .e the !orre!t answer. In
!ontrast, !hoi!e %d' would e0plain a protein O that is a.le to .ind to protein 2 only at
hih temperatures, and would result in a strain that would turn pin4 only at hih
temperatures. )hoi!e %a' would produ!e a protein O that would .ind to protein 2 more
tihtly than the normal protein, and would therefore .e li4ely to .ind %and turn pin4' at
temperatures a.ove 3E). If a !ovalent .ond was made %!hoi!e %!'', it is unli4ely that
su!h a .ond would .e disrupted .y any temperature in whi!h the mi!rooranism !ould
survive= the mi!rooranism would therefore turn pin4 at any temperature. )hoi!e %f'
would result in a strain that !ould not turn pin4 at any temperature.
2(