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Molecules Cells and Variation[XA BY01] > Biological Molecules and Enzymes > Flashcards

Biological Molecules and Enzymes Flashcards

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Organic Chemistry 101 flashcards
1
Q

What ratio is hydrogent to oxygen in carbohydrates

A

2:1

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2
Q

What is molecular formula of 3 main hexose sugar?

A

C6H12O6

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3
Q

Name 3 types of hexose sugar?

A

Glucose
Galactose
Fructose

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4
Q

What is difference between alpha and beta glucose?

A

Alpha has glucose above
Beta has glucose below

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5
Q

What is main 3 disaccharides and what they consis of?

A

Maltose, 2 glucose

Sucrose, 1 glucose and 1 fructose

Lactose, 1 glucose and 1 galactose

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6
Q

Name and describe reaction joining 2 monomers?

A

Condensation reaction

It form chemical bond between 2 molecules releasing 1 water molecule as byproduct

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7
Q

Name and describe reaction breaking a dimer or polymer?

A

Hydrolysis

Chemical bond between 2 molecules is broke by instertion of 1 water molecule

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8
Q

Describe test for reducing sugar?

A

Add benedicts solution to sample

Boil for 5 minutes

A brick red/orange colour if present

If not solution remain blue

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9
Q

Describe test for non-reducing sugar?

A

First test sample with benedicts solution to confirm negative results

Then boil sample with dilute acid

Then cool then add sodium hydroxide solution to neutralise it

Then add benedicts solution and boil

If non-reducing sugar, now red brick colour shoud appear

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10
Q

What is example of non-reducing sugar?

A

Sucrose

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11
Q

What is 4 main similar and different properties of cellulose, starch and glycogen?

A

They differ in num and arrangement of glucose

They function as storage or structural molecules

They are non-reducing

They are unsweet

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12
Q

What is cellulose?

A

Consist of beta glucose

Fromed by 1-4 glycosidic bond so every beta glucose invert

Long, straight chain

Hydroxyl group form hydrogen bond with other chain hydroxyl group called microfibril

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13
Q

What is macrofibrils?

A

Bundle of microfibril

One macrofibril goes in same direction

Succesuve layers are in different direction

They are interwoven and embedded in matrix to provide rigidity

Gaps between layer allow fully permeable cell wall

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14
Q

What is purpose of cellulose?

A

Rigid, structural support preventing cell from bursting

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15
Q

What is starch?

A

Storage used for respiration made by alpha glucose

Found in starch grain of plant

Amylose and amylopectin

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16
Q

What is properties of starch?

A

Long chain of alpha glucose

Compact, helical shape due to hydroxyl group forming hydrogen bond

Amylopecting is branched but amylose is straight

Amylopectin has 1-4 and 1-6 glycosidic bond and amylose only 1-4 glycosidic bond

Insoluble so osmotically inactive

Too large to cross cell membrane but compact

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17
Q

Name and describe test for starch test?

A

Iodine test

Add few drops of iodine to sample

If starch is present blue/black colour appear

If no starch remains orange/yellow

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18
Q

What is glycogen?

A

Energy store in animal and fungi

Same properties as starch but more branched

Mostly liver and muscle tissue

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19
Q

What is 2 types of lipids?

A

Triglycerides and phospholipid

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20
Q

What is properties of triglycerides?

A

Made of 3 fatty acid and 1 glycerol

Insoluble so osmotically inactive

Soluble in various solvent e.g. alcohol but water

Formed by condensation reaction

Has ester bond

Acts as structure and enery storage

Release twice as much energy than carbohydrates

Higher portion of H

Can be saturated or unsaturated

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21
Q

Is saturated solid or liquid?

A

Usually fat

Unsaturated usually oil
As less surface contact of molecule due to bending

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22
Q

Describe and name test for lipids?

A

Emulsion test

Add ethanol to sample

Shake so lipid dissolve

Then add water and mix

White emulsion should appear as indication

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23
Q

What is properties of phospholipid?

A

Made of glycerol, 2 fatty acid and 1 phosphate

Joined by condensation reaction

Polar hydrophilic head is phosphate

Non-polar hydrophobic tail is fatty acid

24
Q

Why is phospholipid important?

A

Cell membrane is formed mainly by phospholipid bylayer

Also form micelles used in lipid digestive absorbtion

25
Q

What element does amino acid contains?

A

C,H, O and N
Sometimes S

26
Q

Properties of amino acid

A

Monomer of polypeptide

All have amine group, a carboxylic group, H attached to C but differ in R group

Theres 20 different R group

Peptide bond joined by condensation reaction

Condensation reactionn is between carboxylic and amine group

27
Q

2 types of enzymes hydrolysing peptide bond and how they differ?

A

Exopeptidases - hydrolyse ends of polypeptide chain

Endopeptidases - hydrolyse internal of polypeptide chain

28
Q

Primary structure

A

Sequence of amino acids in the polypeptide chain, determines the specific shape of the protein

29
Q

Secondary structure

A

H-bond caused by C=O and N-H groups

They can be alpha helix or beta pleated sheet

30
Q

Tertiary structure

A

Ionic, H, disulfide bridge and hydrophobic bonds

31
Q

Quaternary structure

A

More than 1 peptide chain

Held by same bonds as tertiary structure

Maybe assosiated with non-protein/prosthetic groups(e.g. Fe2+)

32
Q

Where does H-bond occurs in amino acid?

A

May form by C=O and N-H groups

Occurs within same chain

May also form between R groups of polar amino acids

33
Q

Check

Where does Ionic bond form in amino acid?

A

Form between + and - charged side chain of bacis and acidic amino acids respectively

34
Q

Where does Hydrophobic region happens in amino acid?

A

Hydrophobic side chains exclude H2O and attracted to each other

35
Q

Where does Disulfide bridge form in amino acid?

A

Oxidation reaction forms it between 2 cystine amino acid

36
Q

2 types of protein?

A

Fiburous and globural

37
Q

Explain what is fiburous proteins and e.g.?

A

Structural function

Insoluble and simple tertiary and quaternary structure made of long parallel chain

Provide strenght and flexibility

Collagen and keratin

38
Q

Explain what is globural protein and e.g.?

A

Highly folded and coiled polypeptide chain forms specific tertiary structure

Soluble in water

Insulin, antibodies, enzymes, receptor

39
Q

What breaks hydrogen bonds?

A

pH, temperature

40
Q

What breaks ionic bonds?

A

pH

41
Q

What breaks disulfide bridges?

A

Reducing agent

42
Q

What is 2 methods to change shape of protein?

A

Heavy metal binding

Denature

43
Q

Describe biochemical test for protein?

A

Add biuret agent to sample

If purple protein present

If remains blue no protein present

44
Q

Define enzymes?

A

Globural protein that acts as biological catalyst with specific active site due to specific tertiary structure

45
Q

How does enzymes work?

A

Lower activation energy

So rate of reaction increase

So more easier for reaction to take place at low temperature

46
Q

Name and describe 2 hypothesis related to Enzymes substrate complex formation?

A

Lock and key hypotheis:
Only substrate with complementary shape to substrate form ESC

Enzymes remains unchanged at end

Induced fit hypotheis:
Enzymes have more flexibility as change shape slightly

Substrate change enzyme active site, and may stain on bonds of substrate so easier hydrolysis

Active site allow molecules to come closer so easier condensation

47
Q

List limiting factor for ESC formation?

A

Enzyme concentration

Substare concentration

Temperature

pH

48
Q

How does enzyme concentration effect ESC?

A

If more enzyme conc, then more active site available

More likely for substrate to collide

So rate increase

If substrate does not limit rate

49
Q

How does substrate concentration effect ESC?

A

More likely for enzymes to collide

Then rate levels off as they saturare active site

So enzyme concentration is limiting factor

50
Q

How does temperature affect ESC?

A

More kinetic energy

So more collision so more ESC

Optimum temperature leads to highest rate

Hydrogen and ionic bond break if too high. leading to denaturation

This alter active site shape

So no ESC

51
Q

Temperature coefficient

A

Rate of reaction at (x+10)/rate of reaction at x

52
Q

How does pH effect ESC?

A

pH different from optimum causes denaturation

As alters ionic charges of acidic and basic groups

So shape of active site change

No longer ESC formation

53
Q

Name 3 types of enzyme inhibitor and how they work?

A

Competitive inhibitor

Inhibitor has similar shape to substrate

So competes with substrate to bind with active site

Reduced by inc substrate concentration

Non-competitive inhibitor

Not similar in shape to substrate

Bind to allosteric sire

Alters tertiary shape and so active site shape

Some would not be able to form ESC or would bind but product dosent form

End-product inhibition

When end product inhibits

It happens when accumulate

So it switch off reaction as builds up

Self-regulatory, so if product decrease switch on

Example of negative feedback

Example is glycolysis

54
Q

What is Immobilised enzymes?

A

Allows to reduce cost and inc efficiency in commercial use

Traps enzymes to plastic support, so recovered easier after reaction

So enzymes can be re-used

Also make enzymes more stable by restricting abillity to change shape or denature

No contamination occurs

55
Q

Example of enzymes that become stable by immobilising them?

A

Glucose isomerase

Stable for a year at 65 degrees celsius in immobilised state but denature whitin few hours at 45 degrees celsius without

56
Q

Physical bonding process in immobilisation?

A

Adsorbed onto an isoluble matrix, e.g. collagen

Held inside a gel, such as silica gel

Held within a semi-permeable membrane e.g. polymer microsphere

Trapped in a micro-capsule e.g. alginate beads

57
Q

Chemical bonding in immobilisation process?

A

Enzymes can be chemically bonded to the support medium

E.g. use glutaraldehyde
to binf it to cellulose fibers

Since enzymes are covalently bonded, enzymes activity is high

Difficult process

Molecules Cells and Variation[XA BY01] (2 decks)

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