Download - Proteins
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PROTEINS
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Proteins are of primary importance to the life of the cell
• by dry weight proteins are the major components of an actively growing cell
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Proteins are constructed of monomers, called:
amino acids
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How do we get the amino acids needed to build proteins?
EATING Protein-Rich Foods
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Proteins ingested are digested by enzymes called……………………proteases
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Non-essential amino acids:can be synthesised by the
body (e.g. cysteine)
Essential amino acids: must be taken in with the
diet the body cannot make them
(e.g. methionine)
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Structure of an amino acid
molecule
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R = Side group/chain [varies]
What is an ‘amino acid’?An organic molecule possessing both carboxyl
and amino groups
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Sometimes books give this [amino acid in solution]:
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The α carbon atom is: the first carbon that attaches to a
functional group asymmetrical
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Amino acids exist in two isomeric forms:
D-amino acids (dextro, “right”)
L-amino acids (laevo, “left”) this form is found in
organisms
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Draw a simple diagram illustrating the arrangement of atoms in a generalised amino
acid. (2)
Question: MAY, 2002
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How many different amino acids:exist:
over 170 are known
are commonly found in proteins: 20
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Amino acids can be grouped based on
side chains
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The various side groups of amino acids
Table 3.2 (Part 1)
NONPOLAR
Leucine
Amino acids are nonpolar.
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The various side groups of amino acids
Table 3.2 (Part 1)
simplest amino acid
POLAR UNCHARGED
Glycine:
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Use your knowledge of biology to explain the following. The discovery of the amino acid glycine in interstellar space has been interpreted, by some scientists, as indicating that life is commonplace in the universe. Other scientists do not share this view.
Question: [SEP, 2006]
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Glycine is one of the 20 amino acids that occur in proteins.
Proteins, in turn are useful organic components of cells.
Proteins play various roles within a cell.
On the otherhand, glycine, is the simplest amino acid, having hydrogen as the radical and could have formed much more easily than the other amino acids.
Complex machinery is required to convert amino acids to functional proteins.
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The various side groups of amino acids
Table 3.2 (Part 1)
POLAR CHARGED
Glutamic acidAmino acids are
polar.
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Table 3.2 (Part 1)
The R-groups also have functional groups:
Arginine [polar, positively charged]e.g. amino group
Glutamic acid:e.g. carboxyl
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The various side groups of amino acids
Table 3.2 (Part 1)
AROMATIC [NONPOLAR]
Phenylalanine
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Let us mention three amino
acids of special interest:
Proline Methionine Cysteine
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Table 3.2 (Part 4)
Proline: causes kinks in chains
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Table 3.2 (Part 3)
Methionine:- is often the first amino
acid in a polypeptide
- contains sulfur
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Table 3.2 (Part 4)
Cysteine: contains sulfur can form disulfide bridges
Sulfhydrl group
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A Disulfide Bridge
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When hair is permed – disulfide bridges in keratin are broken
and reformed
Disulfide bridges in straight hair
Disulfide bridges broken & reformed
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Same happens when hair is straightened
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Why do amino acids differ in their chemical and physical properties (size, water solubility, electrical
charge)? Because of their different R groups
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The side groups of amino acids
determine folding of polypeptide
Table 3.2 (Part 1)
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Side chains of amino acids: show a wide variety of chemical
properties
are important to determine the: 3D structure function of the protein
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hydrophilic amino acids
hydrophobic amino acids
Where do you expect these types of amino acids to be placed in the ion channel spanning the plasma
membrane?
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Ions (black) can only pass through the pore of the ion channel because this is the only part with hydrophilic amino acids lining the pore (green = area of ion channel with hydrophilic water-loving amino acids). The rest of the ion channel mostly consists of hydrophobic amino acids (purple).
hydrophilic amino acids
hydrophobic amino acids
WHY?
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The ORDER of the side chains of amino acids in a protein :
determines how it folds into a three dimensional configuration
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From amino acids to proteinstwo amino acids dipeptidethree amino acids tripeptidemore than 50 amino acids
polypeptide
6 000-1000 000 protein
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Some:need time &a particular
medium
All proteins can be hydrolysed into amino acids
All proteins are broken when:heated in 6M HCl at 115C for several hours
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Let us discover how two amino acids
link together
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H2N
H
H
C C
O
OH
Carboxylgroup
N
H
CH3
C C
O
OHH2N
H
H
C
O
C N CC
HH
CH3
OH
O
Peptidebond
Aminogroup
H
H
H2O
+
Amino acids are joined together by a condensation reaction
A peptide bond is a covalent C-N bond formed by condensation between the -NH2 of one
amino acid and -COOH of another
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H
H H H H H HO O O H H O H H O
N C C N NC C C C
H CH3CH2
OH
N-terminus
N C C
CH2
C
O
OH
CH2
N C C
CHCH3H3C
CH2
OH
H H O
N C C
H H O
N C C
H H O
N C C
CH2
SH
OH
C-terminus
Many amino acids joined together = Polypeptide chain
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Note R groups alternate in the Polypeptide chain
Show the position of a peptide bond
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C-N atoms of the peptide bonds:
lie in the same plane to form the backbone
Side chains of the individual amino acids:are arranged transversal
to each other across the backbone – this confers stability to the molecule
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Question: [SEP, 2000]
The diagram below represents part of the primary structure of one of four polypeptide chains within the haemoglobin molecule.
1. What functional group is present at position X? Amino group
2. What name is given to the bond between two amino acids? Peptide.
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A protein molecule:contains 100’s and 1000’s of amino acids joined
together by peptide links into one or more chains
3 chains in collagen (in mouse tail)
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Polypeptide chains can be folded in various ways
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Proteins are unbranched, not like carbohydrates
Branched molecule
Unbranched moleculeProtein
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Many different types of proteins exist. How can this be?
MILLIONS of Antibodies exist
A LARGE NUMBER OF ENYZMES
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Because any of 20 different amino acids might appear at any position
• E.g. a protein containing 100 amino acids could form any of 20100 different amino acid sequences
• this is 10130, i.e. 1 followed by 130 zeros
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Number and Sequence of amino acids determine the protein
6 amino acids
5 amino acids
7 amino acids
6 amino acids but in a different sequence
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Test for Protein: Biuret Test
Protein present
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Test for Protein: Biuret Test
Cheese is rich in protein.
Add an equal amount of NaOH to the solution
followed by 1-2 drops of CuSO4 solution
pestle
mortar
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Purple / Lilac: Positive test
When a protein reacts with copper(II) sulfate (blue), the positive test is the formation of a
violet colored complex.
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What dictates the function of each protein?The exact sequence of amino acids.
Proteins have many functions:
enzymes
hormones
structural proteins
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DNA contains the information that determines the sequence of amino acids
DNA
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MUTATION
Scrambled sequences of amino acids are useless:
in some cases, just one wrong amino acid can cause a protein to function incorrectly
What is the cause of ‘scrambled sequences of
amino acids’?
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1. PKU (phenylketonuria)2. Sickle cell anaemia
Is the amino acid sequence really important?
Let us illustrate by TWO examples:
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a genetic disorderno enzyme [phenylalanine hydroxylase
(PAH)] is present to process phenylalanine
PKU (phenylketonuria)
phenylalanine builds up – causes mental retardation
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In PKU persons:one amino acid is present instead of
another.
Enzyme that breaks phenylalanine [phenylalanine
hydroxylase (PAH)] has about 452 amino acids.
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A person with PKU must avoid foods that are high in protein, such as:
MilkCheeseNuts Meats
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PKU: no cure
Testing at birth
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Sickle cell anaemiaGlu: Glutamic acid Val: Valine
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At low oxygen levels , haemoglobin S crystallises in the red cells distorting them into a sickle shape.
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Structure of a Protein• each protein has a characteristic three
dimensional shape called its conformation
• four levels of organisation exist:-1) Primary structure2) Secondary structure3) Tertiary structure4) Quaternary structure
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Structure of a Protein
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the number and sequence of amino acids held together by peptide bonds in a polypeptide chain
the primary structure of each
type of protein is unique
Primary structure of a protein:
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Primary structure of insulin: 51 amino acids
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Secondary structure:• the way in which the polypeptide is arranged
in space
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• bonds present: 1. Peptide2. Hydrogen
Two common secondary structures are the:-helix -pleated sheet
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a helix is: in a right-handed coil the most common form of secondary
structure
Secondary structure of many different proteins may be the same
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helix is in a right-handed coil, maintained by H-
bonds between: CO of one amino acid and NH group of the 5th amino acid
Radical groups jut out in all directions
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Keratin: is entirely helical and thus fibrous
hardness & stretchability of keratin varies with degree of disulfide bridges
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-pleated sheet
occurs when two adjacent peptide chains bind to one another
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-pleated sheet chains run parallel but in opposite directions
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-pleated sheet
Side chains stick perpendicular to the plane of the chains assuming a zig-zag pattern
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-pleated sheet
Side chains stick perpendicular to the plane of the chains assuming a
zig-zag pattern
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Silk is an example of a -pleated sheet
Silk Protein Structure
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It is common for a polypeptide to be partly:
- beta pleated sheet
-helix
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Tertiary structure:• is when the polypeptide
chain bends and folds extensively to form a precise compact
• is a complex, three-dimensional shape that determines the final configuration of the polypeptide
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Tertiary structure is determined by interactions of R-groups:
1. Disulfide bonds2. Aggregation of hydrophobic side chains3. Ionic bonds4. Hydrogen bonds
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Further folding of the polypeptide chain contributes to the tertiary structure of a protein
Which amino acid forms disulfide
bridges?
Cysteine
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Hydrophobic Interactions are a major force in the folding of globular proteins
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Myoglobin
153 amino acids in a single polypeptide chain
no disulfide bridges
Haem
molecule is unusual as it consists almost entirely of helices
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Quaternary structure:• the precise arrangement of the aggregation
of polypeptide chains held together by hydrophobic interactions, H-bonds and ionic bonds
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Quaternary structure occurs in many highly complex proteins
A huge variety of quaternary structures exist
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Quaternary structure of various proteins
Antibodies comprise four chains arranged in a Y-shape.
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Quaternary structure of various proteins
Actin- hundreds of globular chains arranged in a long double helix
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Quaternary structure of various proteins
ATP synthase - 22 chains forming a rotating motor.
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The joining of more than one polypeptide chain leads to the quaternary structure of proteins
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Collagen is: a triple helix
a fibrous protein
cannot be stretched due to H-bonds connecting the chains
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Collagen is found in:
cartilage
tendon
cartilage tendons (attach
muscles to bones)
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Collagen is found in:
cornea
the underlayers of skin cornea of the eye
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Haemoglobin:- 574 amino acids - 4 polypeptide chains
-chain
-chain -chain
-chain
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(one molecule of oxygen binds to one haem)
(a) Haemoglobin (b) Iron-containing haem group
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- haem is an iron-containing porphyrin, acting as prosthetic group of several pigments
- prosthetic group is a non-protein group which when firmly attached to a protein results in a functional complex (a conjugated protein)
- porphyrin is a macromolecule composed of four subunits
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How is it possible for foetal haemoglobin to obtain oxygen from
the maternal haemoglobin?
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Foetal haemoglobin is structurally different from that of an adult :
as it has gamma chains instead of beta
What does this difference in structure result in?
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Structural difference results in foetal haemoglobin being able to obtain oxygen from the placenta as it has
a higher affinity for oxygen than the mother’s haemoglobin
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Question: May, 2011 (End-of-Year Exam)Use your knowledge to discuss the biological
significance of the following:
Structure of foetal haemoglobin varies from that of maternal haemoglobin. (5 marks)
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The final three-dimensional shape of a protein can be classified as:
Fibrous Tough Insoluble in water
Globular Soluble
KeratinSilkCollagen
EnzymesAntibodies
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myosin
A few proteins have both structures e.g. the muscle protein :
long fibrous tail
a globular head
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Question: [MAY, 2010]
Use your knowledge of biology to describe the significance of the following. (5 marks)
Proteins have tertiary and quaternary structure.
The tertiary and quaternary structures of proteins create a variety of molecules, each able to carry out a particular function.
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Question: [SEP, 2009]
Why is it mainly proteins that function as enzymes? (2 marks)
Since proteins can twist and fold in many ways, forming a variety of
active site shapes.
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Two Types of ProteinCONJUGATED : globular proteins + non-protein material (prosthetic group)
SIMPLE : only amino acids e.g. albumins, histones
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Name Prosthetic group
Location
Haemoglobin Haem Red blood cellsGlycoprotein Carbohydrate Blood plasmaLipoprotein Lipid Cell membranes
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A protein spontaneously refolds into its original structure under suitable conditions
The loss of the specific three-dimensional conformation (secondary structure) of a protein
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How long can the change be?Temporary or permanent.
Is the amino acid sequence affected?Remains unaffected.
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Why is denaturation of proteins considered as harmful to an
organism?
The molecule unfolds and cannot perform its normal biological
functions.
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Denaturation agents can be:i) Heat
ii) Strong acids & alkalis and high concentrations of salts
iii) Heavy metals (e.g. mercury) iv) Organic solvents and detergents
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i) Heat - weak hydrogen bonds and non
polar hydrophobic interactions are disrupted
- Why?
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Heat increases the kinetic energy
Causes the molecules to vibrate so rapidly and violently that
bonds break
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protein coagulates
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ii) Strong acids & alkalis + high concentrations of salts
ionic bonds are disrupted
the protein is coagulated
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Coagulation of milk by adding salts
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Breakage of peptide bonds may occur if the protein remains in the reagent for a long time
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iii) Heavy metalscause the protein to precipitate out of the
solution
Cations (+) form strong bonds with carboxylate anions (COOH-) and often disrupt ionic bonds
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disrupt hydrophobic interactions
form bonds with non-polar groups
this in turn disrupts intramolecular H-bonding
iv) Organic solvents & detergents
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Why does the solution become purple when beetroot discs are placed in detergent?
1. Proteins in cell membrane & tonoplast are denatured.
2. Phospholipid bilayer is damaged.
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Why is the skin wiped with alcohol before an injection is given?
Alcohol is used as a disinfectant.It denatures the protein of any bacteria present on the skin.
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Question: [MAY, 2004]
1. What change has a protein undergone if it has been denatured? (3)
When a protein is denatured it loses its three dimensional shape in space. Its tertiary structure is destroyed and cannot fold properly. Hydrogen bonds, ionic bonds and hydrophobic interactions that are useful to determine the final shape of the molecule are destroyed.
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Question: [MAY, 2004]
2. List TWO agents that may cause denaturation of a protein. (2)
Extreme changes in pHHeatHeavy metalsOrganic solventsDetergents
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Buffering capacity of proteins
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A buffer can donate or accept H+ to stabilise the pH.
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Why are buffers needed?To keep solution at a constant pH.
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The need of buffers in organisms
Reactions in cells change pH
in blood.
Proteins change shape if pH changes.
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Name THREE buffers in organisms:
Hydrogen carbonate
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Buffering capacity of amino acids
Zwitterion: a compound with both acidic and basic groups
Isoelectric point is that pH at which a zwitterion carries no net electrostatic charge
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Buffering actions by phosphate and hydrogen carbonate
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Functions of Proteins
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Functions of Proteins
Type Example Occurrence / functionStructural Collagen Component of bone,
tendons, cartilage
cartilage
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Functions of Proteins
Type Example Occurrence / functionStructural Keratin Skin, feathers, hair,
nails, horns
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Functions of Proteins
Type Example Occurrence / functionStructural Elastin Elastic connective tissue
(ligaments)
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Functions of ProteinsType Example Occurrence / functionStructural Fibrin
Viral coat proteins
Forms blood clots
‘Wraps up ‘ nucleic acid of virus
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Functions of ProteinsType Example Occurrence / function
Enzymes Hydrolytic enzymesProteases
Cleave polysaccharidesBreak down proteins
Hormones Insulin Regulate blood sugar level
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Functions of ProteinsType Example Occurrence / functionTransport Haemoglobin
Myoglobin
Carries O2 and CO2 in bloodStores O2 in muscle
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Functions of Proteins
Type Example Occurrence / functionTransport Serum albumin
Cytochrome
Transport in blood e.g. lipidsElectron transport
Lipoprotein
Electron carriers
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Functions of ProteinsType Example Occurrence / functionTransport Membrane
transporters e.g. glucose transporters
Transport sugars into cells
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Functions of Proteins
Type Example Occurrence / functionProtective Antibodies Mark foreign proteins
for elimination
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Functions of ProteinsType Example Occurrence / functionProtective Fibrinogen
Thrombin
Precursor of fibrin in blood clottingInvolved in clotting mechanism
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Functions of ProteinsType Example Occurrence / functionMotion Myosin
Actin
Contraction of muscle fibresContraction of muscle fibres
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Functions of Proteins
Type Example Occurrence / function
Storage Caesin Stores ions in milk
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Functions of Proteins
Type Example Occurrence / function
Storage Ferretin Stores iron, especially in spleen
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Type Example Occurrence / function
Toxins Bacterial neurotoxins
Prolonged muscle contraction
Patient Suffering From Tetanus. Painting by Sir Charles Bell, 1809.
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Functions of Proteins
Type Example Occurrence / function
Antifreeze Glycoproteins In arctic flea
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Functions of ProteinsType Example Occurrence / functionReceptors Rhodopsin Light receptor in retina
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Proteins are perhaps the most important group of chemicals in living things. Evaluate this statement. [1995]
Proteins are the working molecules within the cell. Discuss. [MAY, 2000]
Give an overview of the different levels of structural organisation in protein molecules. [SEP, 2004]
Essay Titles
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THE END