[June 2004, P2, Q3]

(a) The table below includes statements about the roles of water
in living organisms
as an environment for living organisms
!om"lete the table b# indicating with a tic$ %& which one of the "ro"erties of water is
res"onsible for each role
'ou should "ut onl# one tic$ in each row
"ro"erties of water
roles of water
high s"ecific
heat ca"acit#
strong cohesive
forces between
water
molecules
high heat of
va"ori(ation
solvent for "olar
molecules and
ions
trans"ort medium
in blood "lasma
and "hloem

surface for small
insects to wal$ on

ma)or com"onent
of sweat used in
heat loss

trans"iration "ull
in *#lem

"reventing wide
variations in
bod# tem"erature

[+]

[Total, +]
[-ov 2004, P2, Q2]
.ig 2/ shows a 0 glucose molecule
Fig. 2.1
(a) 1tate how glucose differs from 0 glucose as shown in .ig 2/
* -OH is below/AW (-H) on carbon (atom)
[/]
(b) .ig 22 shows a molecule of 0 glucose that is about to be added to the end of a growing
chain of a "ol#saccharide
Fig. 2.2
(i) -ame the bond E
* (1-4) glycosidic
[/]
(ii) 2se the diagram below to show how the 0 glucose molecule will attach to the end of
the growing chain of the "ol#saccharide 'ou ma# annotate the diagram if #ou wish
* -OH on free molecule and end of chain indicated
* water eliminated/remoed/condensation reaction
* o!ygen bridge/glycosidic bond drawn in correct "osition relatie to chain
* between #1 and #4$ must be labelled either side of glycosidic bond
[3]
(iii) -ame a "ol#saccharide that is formed entirel# from 0 glucose molecules in the
wa# shown in .ig 22
* cellulose
[/]
[Total, 3]
[-ov 200+, P2, Q2]
Phos"holi"ids are com"onents of cell surface membranes
(a) 4escribe how "hos"holi"id molecules are arranged in a cell surface membrane
'ou ma# use the s"ace below for a sim"le annotated diagram if #ou wish
* %ilayer/two layers
* Hydro"hilic "art/"olar head/"hos"hate/choline$ faces$ water/outside
cell/tissue fluid/cyto"lasm
* Hydro"hobic "art/fatty acid chains$ face each other/AW
[2]
.ig 2/ shows the structure of the li"ids,
tristearin, which is a trigl#ceride5
"hos"hatid#lcholine, which is a "hos"holi"id
Fig. 2.1
(b) 1tate two wa#s, visible in Fig. 2.1, in which "hos"hatid#lcholine differs from tristearin
&hos"holi"id has
* &hos"hate/"hos"horus
* 'wo fatty acid chains
* (atty acids of different lengths) (different numbers of carbon atoms in
each chain)
* *ifferent fatty acids/one is unsaturated/one has a double bond
* #holine/nitrogen/base
[2]
(c) 6*"lain how the structure of trigl#cerides, such as tristearin, ma$es them more suitable
for energ# storage than carboh#drates, such as gl#cogen
* +ong hydrocarbon chain/mostly #H, units re"eated/many #-H bonds -Allow
many #-H bonds.
* Higher "ro"ortion of hydrogen/more highly reduced/few o!ygen/AW
* /enerates much energy (when res"ired)/twice as much energy as
carbohydrate
* #om"act
* #an be stored in anhydrous form
* Higher calorific alue/more energy "er unit mass/smaller mass "er unit
energy
[2]
[Total, 3]
[June 2003, P2, Q4]
.ig 4/ is an electron microgra"h of a chloro"last from a meso"h#ll cell in a leaf
Fig. 4.1
(a) !alculate the magnification of the electron microgra"h in .ig 4/
* (calculation) 10$111 / 120
* (answers) ! 31$111
7nswer 8 999999999999[/]
(b) 1tate two features visible in Fig. 4.1 that identif# the organelle shown as a chloro"last
* starch grain
* grana / thyla4oids / internal membranes
* sha"e$ 5ualified) 6ty"ical chloro"last sha"e7 is minimum acce"table
[2]
(c) !hloro"lasts absorb "hos"hate ions from the surrounding c#to"lasm 1uggest one wa# in
which chloro"lasts use "hos"hate ions
* *8A / 98A / nucleotides / named nucleotide
* "hos"horylated sugars / triose "hos"hate
* "hos"holi"ids
* A'&
[/]
(d) 1tarch grains in "lant cells contain both am#lose and am#lo"ectin
6*"lain how both of these substances are formed from glucose in "lant cells
* condensation (reaction) / described as elimination of water
* glycosidic$ bond / lin4
* 1:4 in$ amylose / amylo"ectin / both
* amylose$ heli! / unbranched
* 1:; lin4s (to gie branches)
* amylo"ectin$ branched
[4]
(e) 1tate three functions of the water stored in the vacuoles of "lant cells
* (raw material) for "hotosynthesis
* maintains turgidity / "roides su""ort
* "ushes chloro"lasts to edge of cell
* used in hydrolysis reactions
* solent for$ ions / named ion / "igment / named "igment
[3]
[Total, //]
[June 200:, P2, Q3]
.ig 3/ shows seven biological molecules, labelled D to K
Fig. 3.1
(a) Table 3/ contains statements about the biological molecules in .ig 3/
!om"lete the table b# selecting the biological molecule from .ig 3/ that matches each
of the statements ;rite the a""ro"riate letter from .ig 3/ in the table The first one has
been done for #ou
'ou ma# use each letter once, more than once or not at all
Table 3.1
statement letter
an amino acid that is a ma)or constituent of collagen J
a com"onent of <-7
/
a molecule that is "ol#merised to form gl#cogen
*
a molecule with a "e"tide bond
H
an im"ortant store of energ#, insoluble in water
<
a molecule with h#dro"hilic and h#dro"hobic regions
(
an amino acid that forms disulfide %disul"hide& bonds in "roteins
=
[3]
(b) 4escribe two wa#s in which the structure of 4-7 differs from the structure of collagen
*8A // collagen
* 4 (different) monomers // more than four (different) monomers
* (monomers >) nucleotides / "olynucleotides // (monomers >) amino acids /
"oly"e"tides
* double heli! / two strands // tri"le heli! / three stands
* loose heli! // tightly coiled
* sugar // no sugar
* "hos"hate / "hos"horus // no "hos"hate / "hos"horus
* base(s) // no base(s)
* "hos"hodiester bonds // "e"tide bonds
[2]
[Total, :]
[-ov 200:, P2v/, Q+]
(a) Table +/ contains statements about four molecules
!om"lete the table b# indicating with a tic$ %& or a cross %& whether the statements
a""l# to haemoglobin, 4-7, "hos"holi"ids or antibodies
'ou should "ut a tic$ or a cross in each bo* of the table
Table .1
statement haemoglobin 4-7 "hos"holi"ids antibodies
contains iron
contains
"hos"hate

able to re"licate
h#drogen bonds
stabilise

the molecule
contains nitrogen

[+]
(b) ;ater is sometimes described as "roviding an ideal environment for man# organisms
6*"lain how the h#drogen bonds between water molecules affect the "ro"erties of water
and hel" to ma$e water an ideal environment for man# organisms
* ref to molecules held together / strong attraction / AW
* detail of hydrogen bonding$ e2g2 slight 2e charge on O$ slight ?e charge on
H
* high boiling "oint / boils at 111o#
* high latent heat of a"orisation
* so water is li5uid oer wide range of tem"eratures
* (li5uid so) "roides$ su""ort / buoyancy
* high (s"ecific) heat ca"acity
* stable tem"erature / tem"erature of water does not change 5uic4ly
* large amount of energy needed to be transferred from water for it to
free@e / high latent heat of fusion
* ma!imum density at 4 A# / less dense at 1 A#
* "roides surface tension
* ref solent
[+]
[Total, /0]
[-ov 200:, P2v2, Q2]
Pol#saccharides, such as gl#cogen, am#lo"ectin and am#lose, are formed b# "ol#merisation
of glucose .ig 2/ shows "art of a gl#cogen molecule
Fig. 2.1
(a) ;ith reference to .ig 2/,
(i) describe how the structure of gl#cogen differs from the structure of am#lose5
* branched
* 1$; glycosidic$ lin4s / bonds
* not$ coiled / helical
[2]
(ii) describe the advantages for organisms in storing "ol#saccharides, such as gl#cogen,
rather than storing glucose
* com"act so large 5uantity can be stored
* insoluble so no osmotic effect
* glucose would lower water "otential
* (so) water would enter and cell olume would increase
* (so) "lant cells would need thic4er cell walls / animal cells might burst
* glucose reactie molecule
[3]
(b) =l#cogen ma# be bro$en down to form glucose
.ig 22 shows region > from the gl#cogen molecule in .ig 2/ in more detail
Fig. 2.2
4raw an annotated diagram in the s"ace "rovided to e*"lain how a glucose molecule is
formed from the free end of the gl#cogen molecule shown in .ig 22
* o!ygen bridge / glycosidic bond$ bro4en
* at left hand end of chain
* water shown to be inoled
* free glucose molecule with -OH drawn on #1
* chain now ends with -OH on #4
[3]
[Total, :]
[June 20/0, P2/, Q/]
(a) .ig // shows the brea$down of a molecule of sucrose
Fig. 1.1
(i) -ame the bond indicated b# T
* glycosidic )
[/]
(ii) 1tate the name given to this t#"e of reaction in which water is involved
* hydrolysis / hydrolytic )
[/]
(iii) 1tate two roles of water !ithin "lant cells other than ta$ing "art in brea$down
reactions
assume that the answer refers to within the cell unless told otherwise
* solent / medium for reactions )
* trans"ort medium )
* maintaining turgidity / 4ee"ing firm / "reents flaccidity / AW )
* (raw material / reactant for) "hotosynthesis / "hotolysis )
* e!"ansion / elongation / growth )
* maintains$ hydrostatic "ressure / "ressure "otential )
* maintains water "otential (gradient) ) A maintains osmotic gradient /
"reents "lasmolysis
* stomatal o"ening )
* hydro"hilic interactions of membranes )
* (in acuole) "ushes chloro"last to edge of cell )
* 9 hydrogen bonding un5ualified by ref2 to membranes
[2]
[June 20/0, P22, Q4]
.ig 4/ shows the "rimar# structure of a l#so(#me molecule, an en(#me found in tears, saliva
and in l#sosomes
Fig. 4.1
(a)
(i) 6*"lain what is meant b# the term "rimar# structure
* (describes the) se5uence of amino acids (in a "oly"e"tide chain) ) A
order/arrangement
[/]
(ii) The molecular structure of the first two amino acids of l#so(#me, l#sine and valine, is
shown below
2se the s"ace to show how these amino acids become lin$ed in a condensation
reaction
* H,O/water$ released )
* (correct) bond formation between (lysine) carbo!yl grou" and (aline)
amino grou" )
* di"e"tide (of lysine and aline) and formed with correct structural formula
[3]
(b) Proteins, such as the en(#me l#so(#me, have a secondar# structure and a tertiar#
structure
(i) 4escribe the secondar# and tertiar# structure of an en(#matic "rotein, such as
l#so(#me
secondar#
* regular order/"attern$ based on H-bonds )
* between #OB grou" of one amino acid and 8HB grou" of another )
* al"ha-heli! and C-"leated sheet )
[2]
tertiar#
* folding coiling )
* interactions between$ 9 grou"s side chains )
* two correctly named bonds ) e2g2 hydrogen bonds$ disulfide$
bonds/bridges$ ionic bonds$ hydro"hobic interactions
* further descri"tion of bonds ) e2g2 disulfide between cysteine (DBH)
grou"s hydrogen between "olar grou"s (8HB and #OB) ionic between
ionised amine and carbo!ylic acid grou"s hydro"hobic interactions
between non-"olar side chains
* ref2 actie site$ s"ecific/"recise$ sha"e )
* ref2 globular/AW$ sha"e ) A s"herical/ball
* ref2 amino acids with$ hydro"hilic/"olar$ 9 grou"s facing to outside ) ora
[3]
(ii) 1tate wh# it is im"ortant for en(#mes, such as l#so(#me, to "ossess a tertiar#
structure
* enables ("rotein to) function/AW ) A enables antimicrobial action/AW$
A biological catalyst$ 5ualified
* "roides actie site )
* 5ualified ref2 to s"ecificity )
[/]
(c) 1ome "eo"le have a rare disease caused b# a single change in the 4-7 nucleotide
se?uence of the gene coding for l#so(#me The change leads to the formation of an
insoluble "rotein that has a different structure to the normal soluble l#so(#me molecule
1uggest how a change in the gene can lead to the differences observed between the
normal l#so(#me and the changed l#so(#me
* altered$ (m98A) codon(s)/tri"let(s) ) A named ty"e of mutation
* changed/AW$ amino acid(s) )
* ref2 to effects of sto" codon ) e2g2 shortened "oly"e"tide chain
* different$ "rimary structure/described ) A ref2 to differences in$
transcri"tion/translation
* ref2 to different "ro"erties of$ 9 grou"/side chain (of normal re"laced
amino acid) )
* altered tertiary structure/AW ) A different 9 grou" interactions$ A
change/loss of$ actie site
* idea of globular to fibrous change/hydro"hilic 9 grou"s no longer to
outside
[3]
[Total, /3]
[June 20/0, P23, Q3]
The amino acid se?uence of the "rotein hormone insulin is shown in .ig 3/
Fig. 3.1
(a) ;ith reference to .ig 3/, state
(i) which two levels of "rotein structure are shown
* "rimary ) A first
* 5uarternary ) A fourth
[2]
(ii) the name of the structures res"onsible for holding the two "ol#"e"tide chains together
* disulfide (bonds/bridges) )
[/]
(b) @an# "eo"le with diabetes need to ta$e regular in)ections of insulin Ansulin in the form
shown in .ig 3/ cannot be ta$en b# mouth as it would be h#drol#sed b# "roteases in the
gut
An the s"ace below, draw a diagram to show how the "e"tide bond between glutamine /+
and leucine /3 in "ol#"e"tide chain 7 could be h#drol#sed and show the "roducts of the
h#drol#sis
* "e"tide bond bro4en )
* correct inolement of water )
* free B#OOH/B#OO- and free B8H,/B8H3 ? shown )
[3]
[Total, 3]