Basic Biological Molecules

10.
1 - Biological molecules
Biochemistry is the study of the chemicals of living organisms. Biochemistry gives us an
understanding of how biological systems work.
Organic Compounds of Biological Significance
There are 4 main organic compounds of biological significance
Elements
Carbohydrates C H O
Lipids C H O
roteins C H O !
!ucleic acids C H O
These are macromolecules " giant molecules made from many repeating units# it is therefore called a
polymer
The e$ception to this are lipids %not composed of a repeating unit&
The repeating units are called monomers
The same type of unit can be used to build different types of chains " long' short' straight' branched
Polymer Monomer
Carbohydrates olysaccharide (onosaccharide
roteins rotein )mino acids
!ucleic acids !ucleotides
Lipids are composed of units of fatty acid and glycerol
Carbohydrates
Overhead " Classification of COH from Biol *ci +,- " Copy into notes
.lements in carbohydrates are carbon' hydrogen and o$ygen
T.G. AS Module 1 Core Principles 249122830.doc Teaching o!es Page 1 2"#10#14
There are always twice as many H atoms as O atoms per carbohydrate molecule
/eneral formula 0 %CH
-
1&
n
2unction of carbohydrates is the storage and liberation of energy. ) few e.g. cellulose have a
structural role
Monosaccharides monomers!
)ll monosaccharides are sweet and soluble
The cannot be hydrolysed %B3O4.! 5O6!& to sugars of a smaller si7e
/eneral formula " %CH
-
O&
n
(onosaccharides are classified according to the number of carbon atoms in the molecule
8 carbon molecule " triose monosaccharide
9 carbon molecule " pentose monosaccharide
: carbon molecule " he$ose monosaccharide
/lucose is a monoaccharide " this is the sugar found in animal blood. 2ructose has the same
formula but is a different shape. *ucrose is the most common sugar in plants and is a disaccharide
*ee handout;overhead" structure of monosaccharides
"SOME#"SM
)n important structural characteristic of monosaccharides %e.g. glucose& is the occurrence of
isomerism
<f two different compounds have the same molecular;structural formula they are isomers of each
other
(onosaccharides can vary in the arrangement of the hydro$yl group around the no + carbon atom
..g. when glucose forms a ring structure the hydro$yl group may be present above or below the
plane of the ring structure
H above 0 )lpha
OH group is below the plane of the ring = isomer " glucose
H below 0 Beta
Hydro$yl and hydrogen groups have swapped places
OH group is above the plane of the ring = glucose
*ee Overhead
The e$istence of and isomers leads to greater chemical variety and is of importance in for
e$ample the formation of starch and cellulose
Both types occur naturally and result in considerable biological differences when they form polymers
$etecting monosaccharides
There are a number of simple tests to identify groups of carbohydrates. (ost are effective if carried
out on a solution or suspension of COH.
<f the material is in solid form' it should be ground up with motar and pestle and resultant li>uid
filtered and tests carried out on filtrate. <f heating is necessary use a water bath
)ll monosaccharides are capable of reducing other chemicals such as Cu%<<& sulphate to copper %<&
o$ide.
6hen monosaccharides combine to form disaccharides this reducing ability is often retained with the
result that sugars such as lactose and maltose %although disaccharides& are still reducing sugars.
<n a few cases the formation of a disaccharide results in the loss of this reducing ability. This is true
of sucrose which is a non reducing sugar.
(onosaccharides ? Benedicts solution ? heat " brick red ppt
*oluble copper %<<& sulphate %blue& in the Benedict solution is being reduced to insoluble copper %<&
o$ide %orange red& %Cu
-?
? e
=
0 Cu
?
&. This reduces the valency of copper from - to +. *ome of this
precipitates out in the alkaline Benedict solution %!aOH&
(onosaccharides donate the e
=
therefore all monosaccharides are called reducing sugars
3ole of monosaccharides " They are soluble and can be easily moved around the body. They are
molecules which are small enough to pass through membranes therefore carbohydrates are
absorbed into cells as monosaccharides. They are also used in respiration and they are the transport
unit of CHO
$isaccharides
)ll are sweet' soluble in water and form crystals but can also be hydrolysed %broken down& into
sugars of smaller si7e
%ormation of disaccharides
*ee life sciences on file
+. (onosaccharides align %usually he$oses&
-. Hydrogen atom removed from OH group at position + of monosaccharide
8. Hydrogen atom removed from OH group at position 4 of ad@acent monosaccharide
4. O$ygen atom removed from one of OH groups
9. This results in the formation of a covalent bond. The covalent bond is called a /LACO*<5<C bond
and it @oins the - monosaccharides at positions + ,4 Therefore called a +=4 glycosidic bond
!OT. " The bonding involves the removal of water. This is a dehydration or condensation reaction.
The reactions are controlled by en7ymes.
)ny - monosaccharides may be linked in this way to form a disaccharide of which maltose' sucrose
and lactose are the most common
Condensation
<.e. " /lucose ? 2ructose *ucrose ? H
-
O
Or 5ehydration
*ee diag from CC in Biol ; Overhead
&ypes of disaccharides
*ucrose 0 /lucose ? fructose
Lactose 0 /lucose ? /alactose
(altose 0 /lucose ? /lucose
$etecting disaccharides
(altose and lactose are reducing sugars. *ucrose is a non reducing sugar
5isaccharides can therefore be reducing or non reducing therefore the test for reducing sugars is as
described above.
2or non reducing sugars there is no specific test but they can be detected by their inability to reduce
BenedictBs reagent directly.
<f it is hydrolysed by boiling with dilute HCl it will be broken down into constituent monosaccharides.
These will then reduce Benedicts in the normal way.
Therefore non reducing sugars are identified by a negative reaction to benedicts before hydrolysis
and a positive result after.
Polysaccharides
2unction chiefly as food ; energy stores and structural materials. ..g. starch ; glycogen ; cellulose
)ll polysaccharides are insoluble' unsweet and cannot be crystallised but can be broken down into
sugars of a smaller si7e
%ormation of Polysaccharides
(any monosaccharides combine together %+111Bs&. The number of monosaccharides which combine
is variable and the chain may be branched or unbranched.
The chains may be folded' making them compact' inert and ideal for storage.
The si7e of the molecules makes them insoluble " another feature that suits storage purposes
because it e$erts no osmotic influence on the cells and does not diffuse.
The properties of the polysaccharide depend on the number of monosaccharide units and how they
are @oined together. ..g. glucose can be @oined together in many different ways to form different
compounds
*ee life sciences on file;overhead " formation of starch
+. 5isaccharides align
-. /lycosidic bonds form between ad@acent disaccharides by condensation forming long chain
polysaccharide molecules
&ypes of polysaccharide
)ll the following are polymers of glucose
a&
S&'#C( C
:
(
+1
O
9
!
n
*tarch is a reserve of food formed from any e$cess glucose produced in photosynthesis. .$cess
glucose must be stored as it an important source of energy
*tarch molecule is a long chain of +=4 linked = glucose units. The chain %long' unbranched& is then
coiled into a heli$ forming a cylinder in which most of the OH groups pro@ect to the inside
*hape of molecule = !o bonds form between starch molecules so not very good structurally
2unctions " found in plant cells only
*tarch molecules accumulate to form granules called grains or plastids %common in seeds&
.$erts no osmotic effect because does not dissolve in water
$etecting starch
*tarch ? iodine;potassium iodide Blue;black colour
T.G. AS Module 1 Core Principles 249122830.doc Teaching o!es Page $ 2"#10#14
O3
Hydrolysis
*tarch solution ? )mylase (altose ?(altase 0 )lucose
*+,e -ith Benedicts
B )./CO)E0 C
:
(
+1
O
9
!
n
1 'nimal starch!
/lycogen consists of a long chain of glucose molecules linked by +=4 or +=: glycosidic bonds
2unction " short term storage COH in animals. *tored in muscle and liver cells %centres of high
metabolic activity&. Can form up to +1C of liver mass. /lycogen needs to be converted to glucose
when needed
/lycogen ? /lycogenase glucose
Conversion is controlled by hormones
*lightly more soluble than starch %shorter chains and more highly branched&' e$ists as granules in the
cytoplasm " close to *.3
C CE..2.OSE
Cellulose consists of long chains of = glucose molecules.
Chains are straight and run parallel with cross linkages in between them. The hydrogen bonds
between the glucose chains are weak but the number of them are what gives the cellulose its
strength. These give cellulose its stability and make it a good structural material. This also makes it
hard to digest
The long straight polysaccharide chains are bonded together by hydrogen bonds to form micelles
The micelles group together to from microfibrils %:1=D1 cellulose molecules& which group together to
form fibres of cellulose %high tensile strength&
Cell walls have several fibre layers running in different directions " again this provides strength
2unctions= structural material in plants e.g. cell walls plant cells " up to 91C of plant cell wall is
cellulose " it is the most abundant organic molecule on earth
Cellulose fibres form a mesh often filled with organic material %matri$&
To make impermeable the matri$ must be plugged %it is of course important that the matri$ is not
plugged in plant cells so the walls remain permeable&
..g. lignin " $ylem
Both impermeable to water
*uberin " bark
(an uses fibres from plants e.g. cotton
T.G. AS Module 1 Core Principles 249122830.doc Teaching o!es Page % 2"#10#14
$etecting cellulose
Cellulose ? *chult7Bs solution 0 purple
O3
Cellulose ? Cellulase glucose %test with Benedicts&
T.G. AS Module 1 Core Principles 249122830.doc Teaching o!es Page " 2"#10#14
P#O&E"0S
lant foods tend to be rich in COH' animal foods tend to be rich in protein and fat.
These are organic compounds with a large ((
!umber of proteins is limitless because there are over -1 different amino acids
roteins are often specific to each species %glucose is glucose in any species but proteins can be
different&. <t is therefore proteins which determine the characteristics of a species.
roteins are rarely stored e$cept in eggs and seeds
.lements in proteins are C H O ! %always&
* %possible&
Structure of a Protein
roteins are chains of amino acids %these are the monomers&. )ll the amino acids %+D1 different
chemicals' -1 commonly occur in proteins& have the same basic structure
)lways haveE
!ote !
-
H 0 !H
-
0 )mino group %basic&
COOH 0 )cid Carbo$yl group %acidic&
*ee fig 8.+9 CC in Biol
)ll amino acids have the same amino group and carbo$yl group and therefore are neutral amino
acids. ) few have an e$tra amino group 0 basic. Others have an e$tra carbo$yl group 0 acidic
They differ in the nature of the 3 group " the group attached to the central C atom
..g. /lycine %simplest known& " 3 group 0 H
)lanine 3 group 0 CH
8
Faline 3 group " C
8
H
D
)ll amino acids are colourless' crystalline solids which are soluble in water where they form ions
*ee life science on file;Overhead
Properties of amino acids
1. B2%%E#"0) 'C&"O0
roteins are buffers %resists tendency to alter pH in acid;alkaline solution& This is due to the structure
of the amino acids subunits in that amino acids have acid and basic properties
The amino group is basic
The carbo$yl group is acidic
Therefore if an amino acid is in acid conditions the H
-
! acts as a hydrogen acceptor therefore
reducing acidity
<f an amino acid is in alkaline condition the carbo$yl group acts as a hydrogen donor %becomes COO&
therefore reducing al3alinity
This property is essential in biological systems where a sudden change in pH could affect en7ymes
Compounds which have both acidic and basic properties are called )(HOT.3<C compounds
therefore aa are amphoteric
4. ESSE0&"'. '0$ 0O0 ESSE0&"'. 'M"0O 'C"$S
*ome amino acids can be synthesised by mammals and are not needed in the diet " !O!
.**.!T)<L )(<!O )C<5*
Certain amino acids cannot be synthesised by man and therefore need to be taken in the diet "
.**.!T<)L )(<!O )C<5*. %G of these& These are made by plants. lants can make all the aa they
need
2ood containing all essential amino acids " first class protein e.g. meat' soya' and pulses5 soya 1
this is ho- ,egetarians can cope -ith a meat free diet!
2ood containing some essential amino acids " second class proteins e.g. veg
.ssential amino acids are no more important than those mammals can synthesis' they are simply
essential because they cannot be synthesised my mammals
6. 'M"0O 'C"$S C'0 BE PO.'#70O0 PO.'#
)mino acids can be classified according to whether they attract;repel water
%O#M'&"O0 O% ' P#O&E"0
*ee life sciences on file;Overhead
+. - amino acids %monomers& align
-. )n OH %hydro$yl group& is lost from the COOH %carbo$yl group& of one of the amino acids and a H
is lost from the amino group %!H
-
& of the other amino acid. ) molecule of H
-
O is removed
%condensation& and the - amino acids become @oined by a peptide bond to form a dipeptide
%covalent carbon=nitrogen bond& 3esult 0 a peptide is formed
8. Continued condensation reactions lead to the addition of more amino acids resulting in the
formation of a long chain of amino acids called a polypeptide chain %a protein molecule&. )
polypeptide chain may be many +11Bs amino acids. The type of polypeptide chain formed
depends upon the se>uence of amino acids in the chain. olypeptides can be linked by peptide
bonds to give proteins of +111Bs of aa
!B the synthesis of polypeptide chains takes place on the surface of ribosomes. %the amino acids
float free in the cytoplasm " taken into the body during absorption& The instructions needed for the
se>uence of the amino acids in the polypeptide come from the 5!) in the nucleus " the information
is transported out to the ribosome in the form of m3!). Once peptide bonds have formed the protein
folds into a particular shape because of 4 other bond types " ionic' disulphide' hydrogen and covalent
bonds
&he primary structure of proteins
roteins have a wide variety of functions and properties. These depend on the type and order of aa
within the protein. There are over +1111 different proteins.
The primary structure of proteins is the type and se>uence of amino acids in the polypeptide chain
and determines the properties and shape of the protein and therefore its biological function. .ach
protein shows a characteristic number and se>uence of amino acids
..g. rimary structure of <nsulin " Biol *ci page HH
The information on primary structure is contained in genes in the nucleic acid %protein synthesis&
&he secondary structure of proteins
This is the shape which the polypeptide chain forms as a result of H bonding. This is the amino acids
in the polypeptide chains interacting
(ost common is an e$tended spiral spring % heli$&
This is the secondary structure. The shape of the molecule is maintained by weak hydrogen bonds
between the loops. H
?
0 electropositive' O 0 electronegative. .ach bond is weak but the number of
them means they have a considerable role in maintaining the shape and stability of the protein. H
bonds are easily broken by high temperatures " this has important conse>uences for living
organisms
&herefore secondary structure is formed -hen a primary structure is modified by coiling5
pleating5 looping etc. Secondary structures are less fle8ible
..g. collagen " triple heli$ " 8 chains put together in a heli$
..g. 5!) %double heli$& " - chains put together in heli$
&ertiary structure of proteins
5ue to bending and twisting of polypeptide heli$ into a compact' globular structure " held together
with weak chemical bonds
6hen a secondary structure e.g. heli$ is folded a more compact tertiary structure is formed with a
definite and precise 85 structure
..g. myoglobin %con@ugated protein&
only protein part shown
Tertiary protein structure is stabilised by
H Bonds
<onic bridges
Covalent bonds
5isulphide bridges
9uaternary structure of proteins
*ome proteins which consist of more than one polypeptide chain e$hibit >uaternary structure. The
linking of polypeptide chains together forms the >uaternary structure. ..g. human haemoglobin is a
protein consisting of - polypeptide chains and - polypeptide chains arranged around an iron
containing haem group
<n general it is the secondary structure which is most important in fibrous proteins which tend to have
structural roles e.g. collagen. <n general it is the tertiary structure which is most important in globular
proteins e.g. myoglobin' en7ymes %see below&
Classification of proteins
Because of the comple$ity of protein molecules and their diversity of function' it is very difficult to
classify them in a single' well defined fashion. One way however is to classify them according to their
structure " as either 2<B3OI* or /LOBIL)3 proteins
2ibrous roteins
<n these proteins it is the secondary structure which is most important %they have little or no tertiary
structure&. They are insoluble in water and physically tough.
They are formed from long parallel polypeptide chains. The amino acids in the chain have a regular
pattern of hydrogen bonds which cause them to coil into long helices that resemble thin springs. The
coils twist round each other' like in a rope. These structures are then cross linked at intervals forming
long fibres or sheets.
This type of protein performs structural functions in cells and organisms. .$amples includeE
collagen %tendons' bones and connective tissue&
myosin %in muscle&
keratin % hair' horn' nails and feathers&
/lobular roteins
<n these proteins the tertiary structure is most important. The polypeptide chains are tightly folded
and bonds between 3 groups at different points make the molecule fold up to form an almost
spherical shape.
This makes it easy for the molecules to move around inside cells or be secreted through membranes.
They are soluble. They form en7ymes' antibodies and some hormones e.g. insulin.
Summary - Properties of proteins
+. can act as buffers because of free COOH and !
-
H groups
-. very large therefore will not go into solution only into colloidal suspension forming viscous sticky
substances
8. protein molecules have a great capacity for attracting;holding water
4. all proteins can be denatured %changed from normal state " loss of 85 shape' aa se>uence
unaffected though& altering the physical;chemical and biological properties of the protein. Can be
temporary or permanent
e.g. protein ? e$cessive heat denatured protein %the H bonds holding
spiral together are destroyed because the atoms in the
protein vibrate more therefore
shape of molecule is irreversibly altered
i.e. spiral opens&
Other denaturing agentsE
*trong acids;alkalis %affects ionic bonds&
)lcohol
)cetone organic chemicals
Irea
*alts of heavy metals e.g. silver ; mercury
(echanical force
5enatured proteins are insoluble
%unction of proteins
+. forming structures for growth' repair' support and movement e.g. cell membranes' hair' nails'
feathers' hooves' tendons
-. buffers
8. transport " haemoglobin " o$ygen
4. proteins can be broken down to release energy %deamination&
9. regulators " en7ymes ; hormones
:. food %nutrition&
D. .n7ymes involved in e$cretion e.g. urease
G. *ensitivity and co=ordination e.g. hormones
H. 3eproductive hormones e.g. prolactin
(ydrolysing en:ymes
roteins can be hydrolysed %by addition of water& breaking the peptide bonds which hold the amino
acid together
rotein ? .n7yme )mino )cids
$etecting proteins
Biuret detects peptide links therefore all proteins are positive.
Biuret " 4OH ? Cu*O
4
urple 0 positive
."P"$S
These are not polymers like COH and proteins but large molecules made of fatty acids and an
alcohol %usually glycerol&
5o contain C H O and @oined by condensation reactions
(ost fat molecules have 8 fa @oined to + glycerol molecule and are called triglycerides
.lements in lipids 0 C H O
They are insoluble in water but dissolve readily in organic solvents like acetone' alcohol
!umber of O atoms relatively small ratio HEO 0 -E+
(a@or function is energy storage. 2at is stored when animals hibernate' it also acts as an insulator.
lants store lipids as oils e.g. in seeds
&ypes of lipids
Lipids
/lycerol based !on glycerol based
*imple Comple$ e.g. wa$es
..g. fats;oils e.g. phospholipids steroids
..g. lecithin
Structure of lipids
Lipids are compounds of an alcohol and fatty acids formed by condensation reactions
(ost common alcohol is glycerol " general formula C
8
H
G
O
8
. /lycerol has 8 OH groups' each of
which can combine with a fatty acid forming a T3</LAC.3<5.. (ost lipids are triglycerides
There is only + type of alcohol in most lipids %glycerol& therefore it is the fatty acids which determine
the characteristics of a lipid
%atty acids
2atty acids have general formula 3 " COOH
3emainder of molecule is a hydrocarbon chain of varying length. This chain is hydrophobic and will
not dissolve in water
- groups
1. Saturated fatty acid
(a$imum number of H atoms " all bonds used. !o double bond in chain. Isually solid at room
temp %animal fats&
..g. stearic acid C
+D
H
89
COOH
Hydrocarbon chain carbo$yl group
+. 2nsaturated fatty acid. (ore than + double bond in chain. Isually li>uid at room temp %plant
fats&
..g. Oleic acid C
+D
H
88
COOH
Oleic acid %chief constituent of olive oil& does not contain ma$imum number of hydrogen atoms
because it has double bond connecting - of the C atoms in the chain
!B oils contain a high proportion of unsaturated fatty acids e.g. linseed oil " D1C unsaturated
2ats contain a high proportion of saturated fatty acids e.g. cocoa butter " D9 saturated
!ote " hydrocarbon chains can be long therefore form the tail 0 The tails are HA53OHOB<C %water
hating& 0 repel water
%ormation of lipids
+. Three fatty acids become aligned beside one glycerol molecule
%the carbo$yl end of the fatty acid points towards the hydro$yl ends %8 in glycerol& of the glycerol
molecule&
-. .ach of the hydro$yl groups of the glycerol molecule loses an h atom
8. .ach of the carbo$yl groups of the 8 fatty acids loses a hydro$yl group
This results in the formation of three o$ygen bonds %ester bonds& and the resulting loss of three
water molecules %ester bonds are therefore formed by condensation&
T.G. AS Module 1 Core Principles 249122830.doc Teaching o!es Page 1$ 2"#10#14
Triglycerides are non polar therefore no uneven distribution of charge in the molecule therefore they
do not form hydrogen bonds with water therefore do not dissolve. They are less dense than water
and therefore float
The lipid which is formed depends on the fatty acids used
&ypes of lipids
a& 2ats " water insoluble. 2atty acids mainly saturated. *olid at room temp
b&
Oils " water insoluble. 2atty acids mainly unsaturated. Li>uid at room temp
c& hospholipids " lipids which contain phosphorus and nitrogen in addition to C H and O
Phospholipids
These are lipids in which + of the fatty acid groups is replaced by phosphoric acid %H
8
O
4
&.
There are therefore - fa and + phosphate group attached to the glycerol.
These are special because phosphoric acid carries an electric charge and is HA53OH<L<C %attracts
water& and will dissolve in water.
The phosphoric acid group is carried in the head of the phospholipid' making the head soluble in
water.
This is in contrast to the rest of the molecule which is hydrophobic %repels water&.
This means that phospholipids float on the surface of the water with the fa tails in the air %will not
dissolve&.
6hen shaken in water the phospholipids cluster together with tails pointing inwards forming a
globule. This characteristic is important in the formation of membranes.
..g. cell membrane
ositive end %water insoluble " hydrophobic&
!egative end %water soluble " hydrophilic&
The addition of a phosphate group gives the lipid polarity %i.e. ?Bve and "Jve ends to molecule
5ue to polarity phospholipids have become part of cell membrane
%unctions of lipids
a& fats;oils
T.G. AS Module 1 Core Principles 249122830.doc Teaching o!es Page 1% 2"#10#14
source of energy " stored fat;oilcan be used in respiration
source of water " released when fat o$idised
heat insulator " when under skin " fat conducts heat very slowly so helping to retain body heat
protects organs " kidneys are embedded in fat
long=term food store " oil in seed " stored because there is a high . yield on breakdown
used to make other molecules like hormones
transport fat soluble vitamins around the body e.g. Fit 5
b& phospholipids
structural " unit membranes
.ipids and the diet
The human body can synthesise most fatty acids from the products of carbohydrate and protein
metabolism.
But there are certain unsaturated fatty acids which man cannot synthesis therefore known as
essential fatty acids e.g. linleic fa; linoleic fa.
2ood which are rich in essential fatty acids are vegetable ; seed oils
&esting for lipids
Emulsion test " add 9cm
8
ethanol and shake. ositive result 0 milky suspension. This is because
being insoluble in water and less dense' oil would float if added to water. Oil here is dissolved in
alcohol within which it is soluble. 6hen water is added the alcohol ? oil mi$es with water

T.G. AS Module 1 Core Principles 249122830.doc Teaching o!es Page 1" 2"#10#14
Chromatography
Chromatography is a common techni>ue used to separate mi$tures of compounds " for e$ample egg
albumin which is a protein made up of several different amino acids
The most commonly used chromatography employs either absorbent paper or a dried thin layer of
powder on glass or plastic.
*pots of the mi$ture are put at one end in a concentrated form then the chromatogram is dipped into
a suitable solvent. The solvent moves through the paper by capillarity until it reaches the spots of
mi$ture.
The compounds in the mi$ture dissolve in the solvent and are carried with the solvent as it soaks
further through the chromatogram.
5epending on its properties each compound will move at a characteristic speed. 6hen the
chromatogram is removed the distance moved by the solvent is marked %solvent front&
*olvent 2ront
Origin
*olvent
Chromatography Tank
The component compounds can be determined using 3f %3elative front& values. .very compound
has a characteristic 3f value
3f value 0 5istance moved by compound
5istance moved by solvent front
.ach amino acid has a characteristic 3f valueE
)mino acid 3f value
Lysine 1.+4
)rginine 1.-1
)spartic acid 1.-4
/lycine 1.-:
*erine 1.-D
/lutamic acid 1.81
Threonine 1.89
)lanine 1.8G
roline 1.48
Tyrosine 1.49
(ethionine 1.99
Faline 1.:1
henylalanine 1.:G
<soleucine 1.D-
Leucine 1.D8
<f egg albumin is digested using trypsin into its constituent amino acids' some of the amino acids
found are glutamic acid' valine' serine' leucine and phenylalanine
&as3;
)ssuming the solvent front moved +-.: cm draw the chromatogram produced by chromatography of
egg albumin

&-o--ay chromatography
Comple$ mi$tures of solutes cannot always be separated efficiently by chromatography in one
direction only.
Thus a further separation must be carried out using a second solvent at right angles to the first for a
better separation of the spots.
) s>uare sheet of paper is used. The test solution is applied to the base line near one end and the
first separation is carried out. The paper is removed' dried and turned through H1o and a further
chromatographic run is made with a different solvent.
)s a result the partially separated solutes of the first run are further separated in the second solute
which has different characteristics from the first.
The paper is removed dried and identification of the solutes can be made
*ee fig )+.: " Biol *ci +,-
<ater
6ithout water life could not e$ist on this planet.
<t is important for - reasonsE
+. it is a vital chemical constituent of living cells
-. it provides an environment for the organisms which live in water
The chemical and physical properties of water are unusual and due mostly to its small si7e' its
polarity and to hydrogen bonding between its molecules
olarity is an uneven charge distribution within a molecule
<n water' one part of the molecule is slightly positive' the other part slightly negative. This is called a
5<OL.
<t occurs because the o$ygen atom has a greater electron attracting power than the hydrogen atoms.
)s a result the o$ygen atoms attract the single electron of the hydrogen atoms' giving the o$ygen a
slightly negative charge
6ater molecules therefore has a weak attraction for each other " with the opposite charges coming
together and causing them to behave as if they were JstickyB like magnets. These attractions are
hydrogen bonds and are constantly being formed and broken and reformed in water. )lthough
individually weak bonds their collective effect is responsible for many of the unusual physical
properties of water
Sol,ent properties
6ater is an e$cellent solvent for polar substances. These include ionic substances like salts which
contain charged ions and some non ionic substances like sugars that contain polar groups like OH
=

%hydro$yl group&
On contact with water' the ions and the polar groups are surrounded by water molecules which
separate %dissociate& the ions from each other. This is what happens when a substance dissolves in
water
6hen a substance is in solution its molecules can move about more freely' making it more reactive "
therefore the ma@ority of the chemical reactions in a cell take place in a>ueous solution
By contrast' non polar molecules like lipids are repelled by water and group together in its presence.
These are HA53OHOB<C
6aterBs solvent properties also mean that it acts as a transport medium' as in the blood' lymphatic
and e$cretory systems
(igh heat capacity
The heat capacity of water is the amount of heat re>uired to raise the temperature of + kg of water by
+
o
C
6ater has a high heat capacity which means a large increase in heat energy results in a relatively
small rise in temperature. This is because much of the energy is used in breaking the hydrogen
bonds which restrict the movement of the molecules
Temperature changes within water are minimised as a result of its high heat capacity
Biochemical processes therefore operate over a smaller temperature range' proceeding at more
constant rates and are less likely to be inhibited by e$tremes of temperature
6ater also provides a very constant e$ternal environment for many cells and organisms
This property means water has a high heat of vaporisation % i.e. needs a lot of . to convert from a
li>uid to a gas& and a high heat of fusion %i.e. needs a lot of . to convert from a solid to a li>uid&
$ensity and %ree:ing Properties
The density of water decreases below 4
o
C and so ice tends to float. <t is the only substance whose
solid form is less dense than its li>uid form
*ince ice floats it forms at the surface first and the bottom last. This has important conse>uences for
organisms living in water in clod climates or with cold seasons
(igh surface tension and cohesion
Cohesion is the force whereby individual molecules stick together
)t the surface of a li>uid' a force called surface tension e$ists between the molecules as a result of
cohesive forces between the molecules
These cause the surface of the li>uid to occupy the least possible area %ideally a sphere&
6ater has a higher surface tension than any other li>uid
<ater as a reagent
6ater is an essential metabolite " that is it participates in the chemical reactions of metabolism. <t is
used as a source of hydrogen in photosynthesis and is used in all hydrolysis reactions

Review Questions:
1. &h' is (a!er considered !o )e a polar *olecule+ &ha! !'pe o, )ond occurs )e!(een (a!er *olecules+
2. -.plain (h' ice ,loa!s on li/uid (a!er. &ha! 0alue does !his ha0e+
3. 1is!inguish )e!(een an acid and a )ase. Gi0e an e.a*ple o, each.
4. Solu!ions (i!h a p2 o, less !han " are !er*ed (hereas !hose solu!ions (i!h a p2 grea!er !han " are !er*ed . As !he
p2 scale decreases3 !here is a
4 ,old increase in h'drogen ion concen!ra!ion ,or e0er' p2 uni!.
$. 1e,ine a )u,,er. &ha! is !he ,unc!ion o, a )u,,er solu!ion+
%. 1is!inguish )e!(een deh'dra!ion s'n!hesis and h'drol'sis.
". &ha! is !he ,unc!ion5s6 o, pro!eins+
8. &ha! are !he 2 ,unc!ional groups in a*ino acids+ 2o( do a*ino acids di,,er+
9. &ha! !'pe o, )ond 7oins 2 a*ino acids !oge!her+ 1escri)e (hich par!s are 7oined.
10. Co*pare a dipep!ide3 a pol'pep!ide3 and a pro!ein *olecule.
11. 1is!inguish )e!(een !he pri*ar'3 secondar'3 !er!iar' and /ua!ernar' s!ruc!ure o, a pro!ein.
12. &ha! is !he di,,erence a*ong *onosaccharides3 disaccharides3 and pol'saccharides.
13. 8is! 2 sugars each ,or *onosaccharides3 disaccharides3 and pol'saccharides.
14. &ha! is !he role o, s!arch3 gl'cogen3 and cellulose in cells+
1$. Are lipids solu)le in (a!er+ 1is!inguish )e!(een ,a!s and oils as !'pes o, lipid. 2o( are !he' ,or*ed+
1%. -.plain !he di,,erence )e!(een a sa!ura!ed and an unsa!ura!ed ,a!!' acid.
1". &ha! is a soap+ &h' does soap cause oil !o disperse in (a!er+ &ha! is *ean! )' e*ulsi,ica!ion+
18. 2o( is !he phospholipid )ila'er arranged in !he cell *e*)rane+
19. &ha! is uni/ue a)ou! !he s!ruc!ure o, s!eroids+ 8is! se0eral e.a*ples o, s!eroids.
20. 8is! 2 !'pes o, nucleic acids. 2u*an genes are co*posed o, (hich !'pe+
21. Gi0e !he co*ponen!s o, e0er' nucleo!ide. &ha! dis!inguishes 1A ,ro* 9A+
Objectives Test
Completion and Short Answer Questions
1. 1e,ine an acid3 )ase3 and sal!.
a. acid

). )ase

c. sal!

2. :, !he h'drogen ion concen!ra!ion ;2
<
= o, 10
4"
has a p2 o, "3 (ha! is !he p2 o, !he ,ollo(ing concen!ra!ions+
;2
<
= p2 Acid or >ase+
a. 10
44
). 10
?%
c. 10
?10
d. 10
? 14
3. &hich o, !he nu*)ers a)o0e represen!s !he larges! ;2
<
= +
4. &ha! is !he i*por!ance o, p2 !o )iological s's!e*s+

$. 2o( do li0ing !hings pre0en! rapid and dras!ic changes in p2+

%. &ha! are !he 4 classes o, )iological 5organic6 *olecules+

". o, !he classes in ans(er 1"3 (hich@
a. are MAST concerned (i!h energ'+
). one ,or*s *os! enB'*es+

c. one *aCes up genes+

d. are long4!er* energ' s!orage+

8. &ri!e !he (ord saturated and !he (ord unsaturated )enea!h !he appropria!e s!ruc!ure.

9. 8a)el !he diagra* (i!h !he ,ollo(ing !er*s@ synthesis, hydrolysis, macromolecule, monomers.
10. &hich $ *olecules in /ues!ion 9 (ould )e associa!ed (i!h par! 5a6 in !his diagra*+

11. &hich 4 *olecules (ould )e associa!ed (i!h par! 5c6 in !his diagra*+

12. &hen *an' glucose *olecules are 7oined3 !he *acro*olecule
resul!s. &hen *an' a*ino acids are 7oined3 !he *acro*olecule
resul!s. &hen gl'cerol and ,a!!' acids are 7oined3 resul!. &hen
nucleo!ides 7oin3 !he *acro*olecules resul!.
13. :n !his h'drol'!ic reac!ion3 (ri!e in !he na*e o, !he *olecule re/uired on !he le,! and !he a!o*s re/uired on !he righ!.
14. The diagra* )elo( is an a*ino acid. &ri!e !he (ord amino and !he (orC acid on !he appropria!e line.
1$. The diagra* )elo( is a dipep!ide. Circle !he pep!ide )ond.
1%. 8e0els o, pro!ein s!ruc!ure.
The linear se/uence o, a*ino acids in a pro!ein cons!i!u!es !he
s!ruc!ure. The !'pe o, )ond !ha! linCs !he a*ino acids is a5n6
)ond. The ,unc!ional groups on a a*ino acid !ha! (ill 7oin !o ,or* !his )ond are !er*ed
. The group !ha!
represen!s !he side chains on !he pro!ein
*olecule is !he . The group !ha! represen!s !he side chains on !he pro!ein *olecule is
!he group.
1". The diagra* )elo( represen!s !he s!ruc!ure o, a nucleo!ide. &ri!e !he (ords3 base, sugar, and phosphoic acid )eside !he
appropria!e s!ruc!ures.
18. a. !his is !he pri*ar'
s!ruc!ure o, a s!rand.
&hich le!!ers represen!s !he )acC)one+
&hich le!!er5s6 represen!5s6 !he ni!rogenous )ase+
). &hich *olecule (ould
!he le!!er s s!and ,or+
&ha! speci,ic *olecule is S in 1A+
T.G. AS Module 1 Core Principles 249122830.doc Teaching o!es Page 2$ 2"#10#14
&ha!
speci,ic *olecule is S in 9A+
&hich nucleic acid (ould
re/uire a dou)le s!rand+
19. Acids ha0e a p2 !ha! is !han "3 (hereas )ases
ha0e a p2 !ha! is
!han ".
20. A! p2 "3 ;2
<
= D ;A2
?
=. >elo( p2 "3 (hich o, !hese is grea!er+
21. An unsa!ura!ed ,a!!' acid con!ains less !han a sa!ura!ed
,a!!' acid.
22. &hen gl'cerol co*)ines (i!h 3 ,a!!' acids3 a
*olecule resul!s.
23. are
lipids con!aining phosphorous !ha! are 0er' i*por!an! in cell *e*)ranes.
24. is !he
spli!!ing o, a )ond (i!hin a larger *olecule )' !he addi!ion o, (a!er.
2$. is !he
ac! o, dispersing one li/uid in ano!her3 as ,a! in (a!er.
Matching@ Ma!ch !he ,ollo(ing ans(ers !o one or *ore o, !he (ords )elo(.
a. a*ino acid 5or *ore !han one6 ). gl'cerol
c. glucose 5or *ore !han one6 d. ,a!!' acid
e. nucleo!ide 5or *ore !han one6 ,. )o!h gl'cerol and ,a!!' acids
A. nucleic acid 3 pro!ein 3
pol'saccharide
dissacharide 3 cellulose
.
>. /uicC energ' 3 gene
3 enB'*e 3
long4!er* s!ored energ' plan! cell (all

C. pep!ide )ond unsa!ura!ed
ri)ose
Gl'cogen h'drogen )ond

h'drocar)on 5onl' h'drogen and car)on6
Matching. Ma!ch !he ,ollo(ing ans(ers !o !he diagra*s )elo(.
a. a*ino acid 5or *ore !han one6 ). gl'cerol
c. glucose 5or *ore !han one6 d. ,a!!' acid
e. nucleo!ide 5or *ore !han one6 ,. )o!h gl'cerol and ,a!!' acids
T.G. AS Module 1 Core Principles 249122830.doc Teaching o!es Page 2% 2"#10#14

T.G. AS Module 1 Core Principles 249122830.doc Teaching o!es Page 2" 2"#10#14

Basic Biological Molecules

Transféré par

Informations du document

Copyright

Formats disponibles

Partager ce document

Partager ou intégrer le document

Options de partage

Avez-vous trouvé ce document utile ?

Ce contenu est-il inapproprié ?

Droits d'auteur :

Formats disponibles

Basic Biological Molecules

Transféré par

Droits d'auteur :

Formats disponibles

10.

Vous aimerez peut-être aussi