B Stu April 13

Prepared by Ms.
Ngoo Le-Na
___________CAL BIOLOGY APRIL 2013_____________________________________________
B BIOLOGICAL MOLECULES
Learning Outcomes
Topic B
(1) Carbohydrates
(a)
describe the ring forms of alpha and beta glucose;
(b)
describe the formation and breakage of a glycosidic bond with reference both to polysaccharides and to
disaccharides including sucrose;
(c)
describe the molecular structure of starch (amylose and amylopectin), glycogen and cellulose and relate
these structures to their functions in living organisms;
(2) Lipids
(d)
describe the molecular structure of a triglyceride and a phospholipid and relate these structures to their
functions in living organisms;
(3) Proteins
(e)
describe the structure of an amino acid and the formation and breakage of a peptide bond;
(f)
explain the meaning of the terms primary structure, secondary structure, tertiary structure and quaternary
structure of proteins and describe the types of bonding (hydrogen, ionic, disulphide and hydrophobic
interactions) that hold the molecule in shape;
(g) describe the molecular structure of haemoglobin as an example of a globular protein, and of collagen as an
example of a fibrous protein and relate these structures to their functions (the importance of iron in the
haemoglobin molecule should be emphasised);
(4) Water
(i)
describe and explain the roles of water in living organisms and as an environment for organisms;
Prepared by Ms. Ngoo Le-Na
BIOLOGICAL MOLECULES
Content
The structure of carbohydrates, lipids and proteins and their roles in living organisms
Water and living organisms
The Building Blocks of life
Polymers and Macromolecules
(1) Carbohydrates
Contain elements of C, H an O
H:O = 2:1
Hydrates of C (in water)
General formula: ______________________
Contain several OH groups
Basic sugar unit: Saccharide
3 main groups: Monosaccharide; Disaccharides; Polysaccharides
Biological Functions and Importance:

Explain how carbohydrates can be used as listed below. Give example(s).
i) Energy source
ii) Structural compounds:

iii) Storage compounds : Plants
Animals
iv) Cell recognition
(a) describe the ring forms of alpha and beta glucose;
1.1 Monosaccharides
Sugar; sweet; dissolve in water
Consist of a single sugar molecule
General formula: (CH2O)n ~ n is between 3-7
Classified according to the no of carbon atoms in each molecule
E.g: Trioses (3C); Pentoses (5C); Hexoses (6C)
Molecular and Structural formulae
E.g. Molecular formula: _______________________
Structural formula: draw the ring forms of and glucose
Ring structure: Chain of C atom is long enough to close up on itself and form a more stable ring structure (C1
joins to Oxygen on C5; C6 not in ring)
Hydroxyl group ,-OH on C1 may be below ring (-glucose) or above ring (-glucose) Isomers
Functions of monosaccharides:
Examples
Triose (C3H6O3);
n=3
Pentose (C5H10O5); n
=5
Glyceraldehydes
Ribose;
Deoxyribose
Functions
Intermediates in respiration
Component in RNA, ATP
DNA
Hexose (C6H12O6); n
Glucose
Energy source, broken down in respiration to produce ATP
=6
Fructose
Synthesis of disaccharide
Galactose
Synthesis of polysaccharide
(b) describe the formation and breakage of a glycosidic bond;
1.2 Disaccharides
Sugars
Two monosaccharide joined together by a process ___________________
_________________molecule released to form a ______________________________bond
Disaccharide formed
Digestion of disaccharide/polysaccharide by a process _____________________
Addition of __________________________________ disaccharide broken back to monosaccharide
Examples of disaccharide
i)
ii)
iii)
Draw diagrams to show formation/breaking of MALTOSE & SUCROSE

(c) describe the molecular structure of starch (amylose and amylopectin), glycogen and cellulose and relate these structures to their
functions in living organisms;
1.3 Polysaccharides
Not sugar
Polymers of glucose formed by condensation of many monosaccharide molecules
Each successive monosaccharide is added by means of _________________ bond

forming macromolecule
E.g of polysaccharides.:
STARCH
Polysaccharide
Monomers
Types of Glycosidic bonds

linkage
Structure: Branched/Unbranched
Amylose
Amylopectin
Compare and Contrast the features of the polysaccharides listed in the table
Polysaccharide
Cellulose
Glycogen
Starch
Monomers
(Types of)
Glycosidic bonds
linkage
Describe the
molecular structure
Storage
Organs/tissues
Function
With reference to the diagram below, Describe how the structure of cellulose does contribute to its strength
(strong and rigid)?

(d) describe the molecular structure of a triglyceride and a phospholipid and relate the structures to their functions in living organisms;
(2) Lipids
A varied group of molecules
Insoluble in water
Easily dissolve in organic solvents

(Benzene, ether and chloroform)
Contain: C, H and O (but ratio of H:O not 2:1)

E.g: Triolein molecule (C57H104O6)
Include : Triglycerides, phospholipids and steroids
True lipids are esters of fatty acids and alcohol
2.1 Triglycerides
Commonly known as fats or oil
Made of :
Glycerol, C3H8O3
~ Alcohol found in lipid
~3 C with 3 -OH group
Fatty acids
~ Long molecules of HC chain
~ Contain acidic group: -COOH (carboxyl group)
~General formula: R-COOH
~ R = HC tail, contain many C atoms
~ Hydrophobic
Show the Formation of a Triglyceride [4m]
Chemical & Physical Properties of Saturated and Unsaturated fatty acids and Lipids
Saturated fatty acids
Unsaturated fatty acids
2.2 Phospholipids
One of the three fatty acids replaced by a polar phosphate group

soluble in water
Head: with the phosphate group (Hydrophilic)
Tail : 2 fatty acid tail (Hydrophobic)
Function:
Draw the structure of phospholipid molecule
2.3 Steroids
Characterized by a C skeleton consisting of 4 interlocking rings
Lipid precursor for steroid synthesis
Types of steroids: Cholesterol; Testosterone; Vit D; Estradiol; Cortison
Functions of Lipid
Function
Energy store/reserve
Description/ Explanations/ examples
Good storage material

Insulation against heat loss
Electrical insulation
Water-proofing
Provides buoyancy
Production of metabolic
water
Cell membranes

(e) describe the structure of an amino acid and the formation and breakage of a peptide bond;
(3) Proteins
Macromolecules, high molecular weight
Contain the elements C, H, 0, N and sometimes S , P
made up 1 or more polypeptide chains of amino acids
The amino acids are joined together by peptide bonds.
Amino acids are arranged in a specific sequence results in Proteins of a great variety, very diverse
3.1 Amino acids
Structure of amino acid
There is a central carbon atom (called the "alpha carbon")
four different chemical groups attached to it:
i)
ii)
iii)
iv)
Central carbon
Amino group
Carboxyl group
Variable/ R group
R
Properties of amino acids

Amino acids are amphoteric/ dipolar/ ZWITTERION, Explain:
Amino acids act as buffers in solutions, resisting wide fluctuation of pH, How?
There are about 20 amino acids commonly found in protein

5 different categories/ groups of amino acids.
1. Non-polar R group (hydrocarbon side chains) : glycine, alanine, valine
2. Polar R grp
: serine
3. Acidic R grp (-ve ly charged)
: glutamic acid
4. Basic R grp (+ vc ly charged)
: arginine
5. Some contain Sulphur
: cystein
3.2 Protein Structures
8
3.2.1 BASICS of proteins

Basic unit/ monomer = ___________________________
The basic structure of a protein is a polypeptide chain
Containing hundreds of Amino acids
joined by ___________________________, via process___________________
3.2.2 Formation of dipeptide

In the space provided, show the formation of dipeptide. [4m]
Amino acids are linked together by joining the amino end of one molecule to the carboxyl end of another to
form peptide bond
Involves condensation water removed
When two amino acids join together a dipeptide is formed
Three amino acids form a tripeptide
Many amino acids (from as few as forty, to a few hundred) join together by means of peptide bonds
to form a polypeptide; in a specific sequence (order), determined by gene
3.2.3 Polypeptide
In a polypeptide there is always one end with a amino group, called the N-terminus / terminal and one end
with a carboxyl group, called the C-terminus / terminal.
There are 20 different amino acids found in proteins, yet over tens of thousands of different possible protein.
This variety is possible because of :
(a)
(b)
(c)
What determines the sequence of amino acids in a polypeptide chain? ______________________________
Desceribe & Explain the Types of BONDS that holds protein structure

(f) explain the meaning of the terms primary structure, secondary structure, tertiary structure and quaternary structure of proteins and
describe the types of bonding (hydrogen, ionic, disulphide and hydrophobic interactions) that hold the molecule in shape;
3.2.4 Levels of protein structure

(1) Primary structure
a) Made up of Linear Sequence of amino acids
b) Joined by _____________________
c) Primary structure determines the proteins
_____________________________________________
(2) Secondary structure

a) The polypeptide may coil into helix OR pleated
sheet
b) Shape held by ________________ bond.
helix :
Describe the structure of a helix.
d) The code for the primary structure of any protein is

contained in the_____________
e) Proteins are regarded as informational macromolecules.
-sheet :
Describe the structure of a -sheet.
(3) Tertiary structure
(4) Quaternary structure
a) This is the 3 dimensional structure formed by the folding up

of a whole polypeptide chain into a compact globular shape /
3D shape
b) Each polypeptide chains are usually globular
b) The way polypeptide chain folds is determined by

interactions between amino acids, which depends on:
c) can arrange themselves into a variety of quaternary

shapes.
i)
a) made up of __________________________
Eg: Haemoglobin (refer section 3.3.1)
ii)
c) Describe how the shape of a tertiary structured protein/
globular protein/ 3D structured protein is being formed.
d) Every protein has a unique tertiary structure, which is

responsible for its properties and function
Eg: shape of the active site in an enzyme / antibody
10

(g) describe the molecular structure of haemoglobin as an example of a globular protein, and of collagen as an example of a fibrous
protein and relate these structures to their functions (the importance of iron in the haemoglobin molecule should be emphasised);
3.3 Globular and Fibrous Proteins

The final three-dimensional shape of a protein can be classified as globular or fibrous.
3.3.1. Globular proteins
Made of chains folded into a compact structure
Shperical, folded into 3D shape
Although these folds are less regular than in a helix, they are highly specific and a particular protein will
always be folded in the same way
If the structure is disrupted, the protein ceases to function properly and is said to be denatured.
eg: enzymes, Insulin, Haemoglobin
Describe the molecular structure of haemoglobin.[4]
3.3.2. Fibrous proteins
Fibrous (or filamentous) structure

Made of long molecules arranged to form fibres (c.g, in keratin)
Several helices may be wound around each other to form very strong fibres
Eg: Collagen
Describe the molecular structure of collagen .[4]
11
Compare between globular and fibrous protein

Fibrous proteins
Globular proteins
Structure
Solubility
Physical strength
Molecule structure
Molecule stability
Amino acid sequence
Functions
Examples
3.4 Classification of protein according to composition

I. Simple proteins
only amino acids, eg albumins, globulin
II. Conjugated proteins
complex compound, consist of globular proteins and non-proteinaceous part (prosthetic group)
eg: Haemoglobin has prosthetic grp ~ HEAM
Other eg : phopsphoproteins ( protein + phosphoric acid )
glycoproteins
( protein + carbohydrate )
lipoproteins
( protein + lipid )
3.5 Factors causing protein denaturation (practical)
3.5.1 Significance of denaturation
Proteins ( enzymes included) can only function effectively over a limited range of temp and pH
( breaking of bonds disrupt conformation , configaration / shape changes, loses its function)
If the protein is soluble, denaturation makes it insoluble, and the protein is inactivated
If the protein is insoluble fibrous protein, it loses its structural strength in denaturation
12

(h) *carry out tests for reducing and non-reducing sugars (including semi-quantitative use of theBenedicts test), the iodine in
potassium iodide solution test for starch, the emulsion test for lipids and the biuret test for proteins; PRACTICAL
(i) describe and explain the roles of water in living organisms and as an environment for organisms;
(D) Water
Features
1) small size
2) polarity bipolar
3) ability to form hydrogen bonds
4.1 Properties of water Explain:
i) A great solvent
ii) High heat capacity
iii) High heat of vaporisation / fusion
iv) High surface tension and cohesion
v) Density and freezing properties
vi) As reagent
vii) Transport medium
13
Chapter B : Biological Molecules tutorial questions

1.
The diagram shows the structure of a molecule.

When these molecules condense to form a polymer, which molecules is produced?
A cellulose
2.
B glycogen
D sucrose
Some microorganisms produce -glucosidase enzymes, but mammals do not.

The presence of these microorganisms in a mammal's digestive system aids in the digestion of which substance?
A cellulose
3.
C protein
B glycogen
C protein
D starch
The diagram shows two molecules of glucose. Four possible bonding positions are labelled p, q, r, s, and t, u, v, w.
When these two molecules condense to form glycogen, where could bonds form?
A
B
C
D
4.
p u or p v
p u or q w
p v or q w
p w or v w
Which description applies to cellulose?

molecule
A
B
C
D
5.
Linear and branched

Linear and branched
Linear and unbranched
Linear and unbranched
glycosidic bond
linkage
-1,6 and -1,4
-1,6 and -1,4
-1,4
-1,6
structure
fibrous
non-fibrous
fibrous
non-fibrous
Diagrams 1, 2 and 3 show the structural formulae of three polysaccharides.
What are the names of these polysaccharides?
A
B
C
D
6.
1
Amylose
Amylose
Cellulose
Glycogen
2
Glycogen
Cellulose
Glycogen
Amylose
3
Ce lulose
G ycogen
Amylose
Cellulose
The following statements are not true except:

A
B
C
D
Unsaturated fatty acids can undergo hydrogenation process.

Fatty acids and lipids lacking double bonds are said to be unsaturated.
Unsaturated fatty acids melt at much higher temperatures.
Most animal fats contain unsaturated fatty acids.
14
7.
How many fatty acid residues are normaly present in a phospholipid molecule?
A1
8.
What is the name of the bond joining glycerol and a fatty acid in the formation of a monoglyceride?
ester
glycosidic
hydrogen
peptide
Which combinations describe a triglyceride?
A
B
C
D
11.
D 4
glycerol
hycrocarbon chain
hydrophilic head
phosphate group
A
B
C
D
10.
C 3
Which part of a phospholipid molecule contributes most to the thickness of a cell surface membrane?
A
B
C
D
9.
B 2
Soluble in water
Provides energy
Produces water when

respired
X
X
The diagram shows a molecule that is found in cell surface membranes.

What is present at X, Y, and Z?
A
B
C
D
X
Phosphate
Phosphate
Protein
Protein
Y
Double-bond carbon chain
Single-bond carbon chain
Glucose
Phosphate
Z
Protein
Double-bond carbon chain
Single-bond carbon chain
Glucose
12.
At which levels of protein structure do hydrophobic interactions occur?

A primary, secondary and tertiary
B primary, secondary, tertiary and quaternary
C tertiary and quaternary
D quaternary only
13.
The following statements describe three orders of structure of a protein molecule.

1
2
3
The molecule consists of two polypeptide chains joined and folded around one another.
The sequence and number of amino acids in each polypeptide chain is known.
The amino acids in each chain are coiled into a helix and held in position by hydrogen bonds.
Which order is described by each statement?

Statement 2
Statement 1
Primary
Secondary
A
Primary
Tertiary
B
Secondary
Tertiary
C
Tertiary
Primary
D
Statement 3
Tertiary
Secondary
Primary
Secondary
15
14.
What does a haemoglobin molecule contain?

four iron (Fe2+) ions attached to each haem group
four oxygen molecules attached to each haem group
four polypeptide chains each with four attached haem groups
four polypeptide chains each with one attached haem group
A
B
C
D
15.
Which one of the following reactions results in the conversion of amino acids to proteins?
A
B
C
D
condensation
phosphorilation
deamination
hydrolysis
16.
Which type of bond maintains the helix shape of secondary protein structure?
17.
A disulphide
B hydrogen
C ionic
D peptide
A peptide bond is formed between
A
B
C
D
18.
Bonds are formed by condensation in cellulose, sucrose and haemoglobin.

What are the names of these bonds?
A
B
C
D
19.
an aldehyde gr up and an amino group

an a dehyde group and an ester group
a carboxyl group and an amino group
a carboxyl group and an ester roup
cellulose
sucrose
haemoglobin
glycosidic
glycosidic
peptide
peptide
ester
glycosidic
glycosidic
ester
ester
peptide
ester
peptide
A student was asked to identify the two food substances in each of three test-tubes.
The table shows the results of the students tests.
Testtube
X
Y
Z
Biuret solution
Purple
Blue
Purple
Reagent added to test-tube

Benedicts solution
Iodine in potassium
iodide
Brick-red
Brown
Blue
Blue-black
Blue
Blue-black
Which conclusion is consistent with the results?

A
B
C
D
Egg white and sucrose had been placed in tube X.

Maltose and starch had been placed in tube Z.
Maltose and sucrose had been placed in tube X.
Starch and sucrose had been placed in tube Y.
16
20.
Food tests are carried out on four solutions.

Which solution contains only sucrose and protein?
Solution
Benedicts Test
Acid Hydrolysis
then Benedicts test
A
B
C
D
Iodine in
potassium iodine
solution
X
X
Biuret test
X
X
Key: = Positive results; X = Negative results

21.
What are the properties of water?
A
B
C
D
Specific Heat
Capacity
low
low
high
high
Latent Heat of
Vapourisation
high
low
high
high
Surface tension
low
high
low
high
Fill in the appropriate answer

A water molecule is said to be (1) because it has a positive and a negative pole as a result of the uneven distribution of (2)
within it, this creates attractive forces called (3) between water molecules, causing them to stick together. This stickiness,
otherwise called (4), of water means that its molecules are pulled inwards at its surface. This property is important in plants;
during water transportation along xylem vessels via a process called (5). Water is able to split large molecules into smaller
ones by a process known as (6). Water is the raw material for the process of (7) in green plants and acts as a (8) in the joints
of animals. Three ions found in bone are (9) and (10, whereas the three needed for maintaining an osmotic balance
across cell membranes are (11, (12 and (13.The element found in haemolglobin is (14, whereas (15 is found in
chlorophyll.
Structured Questions
::Question 1::
Fig.1. shows the reaction to form triglycerides.
(a)With reference to Fig.2.1,
(i)name the molecules A and B .
[2 ]
(ii)state the name of the reaction shown. [1 ]

(b)Animals and plants store triglycerides as energy reserves.
Explain the advantages of storing triglycerides as energy
Reserves rather than carbohydrates, such as starch.[2 ]
Fig.1
17
::Question 2::
Fig. 2.1 shows a glucose molecule.
(a) State how glucose differs from glucose as shown in Fig. 2.1.
....................................................................................................[1]
Fig.2.1
(a) Fig. 2.2 shows a molecule of glucose that is about to be added to the end of a growing chain of a
polysaccharide.
(i) Name the bond E.
...............................................................................................................................................................[1]
Fig.2.2
(ii) Use the diagram below to show how the glucose molecule will attach to the end of the growing chain of
the polysaccharide. You may annotate the diagram if you wish.
(ii) Name a polysaccharide that is formed entirely from glucose molecules in the way shown in Fig. 2.2.
...............................................................................................................................................................[1]
::Question 3::
Starch,glycogen and cellulose are all polysaccharides. They are made from monomers that are joined by covalent
bonds.
Complete the table below to show which of the statements apply to each of the polysaccharides.
Fill in each box using a tick ()to show that the statement applies and a cross (X)if it does not.
[5m]
[5]
18
::Question 4::
Haemoglobin is a globular protein that shows quaternary structure. It is composed of two types of polypeptide,
known as and globin.
(a) Explain how a globular protein differs from a fibrous protein, such as collagen.
(b) globin has a tertiary structure that consists of eight helices arranged to give a precise
three-dimensional shape.
Describe how the precise three-dimensional shape of a polypeptide is maintained.
::Question 5::
(a) The table below includes statements about the roles of water
Complete the table by indicating with a tick () which one of the properties of water is responsible
for each role. You should put only one tick in each row.
[2]
[4]
[5]
19

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Prepared by Ms.

___________CAL BIOLOGY APRIL 2013_____________________________________________

describe the ring forms of alpha and beta glucose;

Prepared by Ms. Ngoo Le-Na

___________CAL BIOLOGY APRIL 2013_____________________________________________

Biological Functions and Importance:

ii) Structural compounds:

(a) describe the ring forms of alpha and beta glucose;

Structural formula: draw the ring forms of and glucose

Prepared by Ms. Ngoo Le-Na

___________CAL BIOLOGY APRIL 2013_____________________________________________

Energy source, broken down in respiration to produce ATP

(b) describe the formation and breakage of a glycosidic bond;

Prepared by Ms. Ngoo Le-Na

Polymers of glucose formed by condensation of many monosaccharide molecules

Each successive monosaccharide is added by means of _________________ bond

Types of Glycosidic bonds

Prepared by Ms. Ngoo Le-Na

___________CAL BIOLOGY APRIL 2013_____________________________________________

Prepared by Ms. Ngoo Le-Na

A varied group of molecules

Easily dissolve in organic solvents

Contain: C, H and O (but ratio of H:O not 2:1)

Include : Triglycerides, phospholipids and steroids

True lipids are esters of fatty acids and alcohol

Show the Formation of a Triglyceride [4m]

Unsaturated fatty acids

Prepared by Ms. Ngoo Le-Na

___________CAL BIOLOGY APRIL 2013_____________________________________________

One of the three fatty acids replaced by a polar phosphate group

Head: with the phosphate group (Hydrophilic)

Tail : 2 fatty acid tail (Hydrophobic)

Draw the structure of phospholipid molecule

Characterized by a C skeleton consisting of 4 interlocking rings

Lipid precursor for steroid synthesis

Types of steroids: Cholesterol; Testosterone; Vit D; Estradiol; Cortison

Description/ Explanations/ examples

Good storage material

Prepared by Ms. Ngoo Le-Na

Properties of amino acids

There are about 20 amino acids commonly found in protein

Prepared by Ms. Ngoo Le-Na

___________CAL BIOLOGY APRIL 2013_____________________________________________

3.2.1 BASICS of proteins

3.2.2 Formation of dipeptide

Prepared by Ms. Ngoo Le-Na

3.2.4 Levels of protein structure

(2) Secondary structure

d) The code for the primary structure of any protein is

(3) Tertiary structure

(4) Quaternary structure

a) This is the 3 dimensional structure formed by the folding up

b) Each polypeptide chains are usually globular

b) The way polypeptide chain folds is determined by

c) can arrange themselves into a variety of quaternary

Eg: Haemoglobin (refer section 3.3.1)

d) Every protein has a unique tertiary structure, which is

Prepared by Ms. Ngoo Le-Na

3.3 Globular and Fibrous Proteins

3.3.2. Fibrous proteins

Fibrous (or filamentous) structure

Describe the molecular structure of collagen .[4]

Prepared by Ms. Ngoo Le-Na

_CAL BIOLOGY APRIL 2013___________________________________

_CAL BIOLOGY APRIL 2013___________________________________

_CAL BIOLOGY APRIL 2013___________________________________

_CAL BIOLOGY APRIL 2013___________________________________

_CAL BIOLOGY APRIL 2013___________________________________

_CAL BIOLOGY APRIL 2013___________________________________

_CAL BIOLOGY APRIL 2013___________________________________

_CAL BIOLOGY APRIL 2013___________________________________

_CAL BIOLOGY APRIL 2013___________________________________

_CAL BIOLOGY APRIL 2013___________________________________

_CAL BIOLOGY APRIL 2013___________________________________

_CAL BIOLOGY APRIL 2013___________________________________

_CAL BIOLOGY APRIL 2013___________________________________