Biological Molecules

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Why is Carbon the base of life ?

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OxfordAQA AS Level Biology

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1

Why is Carbon the base of life ?

As it can make 4 bonds with elements like H , O and N

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2

Monomer

A molecule that can combine with others of the same kind to form a polymer.

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3

condensation reactions

Chemical process in which two molecules combine to form a more complex one with the elimination of a simple substance, usually water.

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4

Hydrolysis

The breaking down of large molecules into smaller ones by the addition of water molecules .

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5

What are 3 types of carbohydrates ?

  • Monosaccharides

  • Disaccharides

  • Polysaccharides

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6

How many carbons can monosaccharides contain ?

3-7 :

  • Triose

  • Pentose

  • Hexose

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7

2 examples of pentoses

  • Ribose

  • Deoxyribose

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8

3 examples of hexoses

  • Glucose

  • Fructose

  • Galactose

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9

3 examples of disaccharides

  • Maltose

  • A

  • Sucrose

  • A

  • Lactose

  • A

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10

what are the 3 non-reducing sugars ?

  • Cellulose

  • Starch

  • Sucrose

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11

what are 3 types of polysaccharides ?

  • Starch

  • Glycogen

  • Cellulose

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12

Starches can be either :

  • Amylose

    or

  • Amylopectin

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13

Cellulose : features

Straight , long , unbranched , layered and bonded by H-Bonds :

  • plant based

  • ß Glucose

  • (1-4) Bonding

  • NOT Branched

  • structural function

  • not soluble

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14

Amylose : features

Unbranched and coiled :

  • Plant based

  • α Glucose

  • (1-4) Bonding

  • NOT Branched

  • Helical

  • Storage Function

  • Soluble

  • Starch it is

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15

Amylopectin : features

Long , branched and sometimes coiled :

  • Plant based

  • α Glucose

  • (1-4) and (1-6) Bonding

  • Branched (per 20 subunit)

  • Storage Function

  • Not soluble

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Glycogen : Features

Short , highly branched and sometimes coiled :

  • Animal based

  • α Glucose

  • (1-4) and (1-6) bondings

  • highly branched ( per 10 subunit )

  • Storage function

  • Mostly soluble

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17

Benedict’s test for monomers :

  • add the food sample to water and grind it up

  • add Benedict’s reagent

  • buffer solution for low pH and heat

  • if turns brownish-red —> reducing sugar is present

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18

Reducing sugar

Sugars capable of donating electrons to other chemicals.

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19

Benedict’s test for disaccharides :

  • first apply Benedict’s test to prove there’s no reducing agent present.

  • add HCl to cover disaccharides into monomers.

  • add sodium hydrogencarbonate ( a base ) to bring the solution back to alkalinity.

  • reapply the test and prove that this time reducing agents are present!

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20

Isomer

Compounds that have the same molecular formula but different structures.

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21
<p>what type of glucose is this? </p>

what type of glucose is this?

Alpha Glucose

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22

Glucose : Features

  • Highly soluble

  • Blood sugar it is

  • the first sugar used in humans in order to produce energy

  • controlled by insulin and glucagon

  • produces in plant cells

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23
<p>what type of glucose is this? </p>

what type of glucose is this?

Beta Glucose

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24

fructose : features

  • fruit sugar

  • plants produce it

  • humans can turn it into glucose

  • sweetest sugar

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  • glucose + glucose —>

  • glucose + fructose —>

  • glucose + galactose —>

  • Maltose ( malt sugar )

  • Sucrose ( table sugar )

  • Lactose ( milk sugar )

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27

chemical test for the presence of starch

  • Iodine / Potassium Iodide

  • if turns black —> (+)

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28

3 types of lipids

  • triglycerides

  • waxes

  • phospholipids

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29

lipids : features

  • insoluble in water

  • soluble in non-polar material like acetone, chloroform and alcohols

  • proportion of O to C and H is less relatively

  • used as energy source ( 2x of what carbs give away )

  • waterproof

  • bad conductors of heat

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30
<p>name the parts : </p>

name the parts :

  • glycerol

  • fatty acids

    —>

  • triglyceride

    (+ 3 water )

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31

how many types of fatty acids are there

more than 70

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32

saturated fatty acids

no double bond between carbons

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33

unsaturated fatty acids

containing double bonds between fatty acids

( this results in bending of the molecule thus they are found as liquids in nature )

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34
<p>name the parts of a phospholipid </p>

name the parts of a phospholipid

knowt flashcard image
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35

Emulsion test

  • add lipid to ethanol

  • mix

  • add water

  • if turns cloudy white —> (+)

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36
<p>name the parts </p>

name the parts

knowt flashcard image
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37

the bondings in the secondary structure :

H bonding :

( between carboxyl and amino groups )

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38

the bondings in the tertiary structure :

  • disulfide bonds —> R groups

  • hydrogen bonds —> amine groups, alcohol groups, and acids

  • ionic bonds —> two side and r groups

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39

prosthetic group

non-peptide (non-protein) compounds that mostly attach to proteins and assist them in different ways.

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40

primary structure

the sequence of aa’s that makes up the polypeptides of a protein

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41

secondary structure

the way in which the chain of aa’s of the polypeptides of a protein are folded ( via H-Bonds )

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42

tertiary structure

the folding of a polypeptide chain in a precise way as determined by the aa of which it is composed .

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43

Quatendary structure

a number of polypeptide chains linked together and smt associated with non-protein groups to form a protein.

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44

peptide bond

the chemical bond formed between 2 aa’s during condensation .

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45

active site

a group of aa’s that makes up the region of an enzyme into which the substrate fits in order to catalyze a reaction .

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46

Biuret test

  • to find proteins

  • (+) —> lilac

  • (— )—> blue

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47

covalent bond

a type of intramolecular bond in which atoms share a pair of electrons , one from each atom .

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48

denaturation

permanent changes due to the unravelling of the 3-d structure of a protein as a result of factors such as TEMP change or pH change .

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49

enzyme

a protein or RNA that acts as a catalyst and so alters the rate of reaction .

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50

H-bond

the chem. bond formed between the positive charge on a H atom and negative charge on a another atom of an adjacent molecule .

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51

Ions

a group of atoms that have lost or gained one or more electrons .

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52

isotope

variations of a chemical element that have the same number of protons while having different numbers of neutrons thus having different masses !

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53

mono-unsaturated fatty acid

FA that possesses a carbon chain with a single double bond

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54

oxidation

loss of electrons

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55

reduction

the gain of electrons

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56

polyunsaturated FA

FA that possesses carbon chains with many double bonds .

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57

Key and Lock theory of enzymes

The lock and key model is a theory of enzyme action that explains how enzymes fit their substrate. The active site of an enzyme is structured to fit a specifically shaped substrate. Once the substrate binds to the active site, the enzyme will facilitate the reaction and release products of the reaction.

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58

induced fit model of enzymes

The induced-fit model states a substrate binds to an active site and both change shape slightly, creating an ideal fit for catalysis. Enzymes promote chemical reactions by bringing substrates together in an optimal orientation, thus creating an ideal chemical environment for the reaction to occur.

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59

competitive inhibitor

  • blocks the active site ( compete for it )

  • non permanently bonds with AS

  • when the substrate conc increase , it’s effects decrease

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60

non-competitive inhibitor

  • binds the allosteric site

  • distort the AS

  • permanent

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61

the difference alpha and beta glucose

  • the position H and hydroxyl groups on the carbon atom 1 is inverted !

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62

cellulose adaptations

  • Beta glucose

  • form long, unbranched, straight sheets

  • layered

  • interact and connected by H-Bonds

  • Microfibrils

  • provide strength, steardiness and rigidity

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63

starch adaptations

  • compact

  • helical

  • insoluble ( so does not affect the water potential )

  • hydrolysis lasts shorter than of the cellulose’s

    ( faster delivery of energy )

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64

ES complex

the temporary molecule made when substrate bonded to enzyme .

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65

the affect of pH on protein

  • ph low

  • H+ high

  • ionic bonds disrupted

  • tertiary structure broken

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66

Amino acids in enzymes

The monomers that make up the active site ( or the whole molecule )

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67

Triglycerides are Monomers/Polymers

Monomers as they ( themselves ) have got no monomer or repeating smaller units !

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68

PH probe e

A pH meter is a scientific instrument that measures the hydrogen-ion activity in water-based solutions, indicating its acidity or alkalinity expressed as pH .

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69

Why not all enzymes fit all substrates ? (3p)

  • specific AS due to their specific 3-D structure

  • Only some of the proteins have complementary shapes to these AS ( not fit )

  • So ES complex is formed between specific types of molecules

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70

Is ther any starch molecule found in the human blood ?

NEIN

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71

Why a change in the DNA changes the type of the enzyme ? (3P)

  • DNA change results in a different aa sequence

  • So different bonds formed between aa’s resulting in a different folding .

  • So eventually the AS changes !

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