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Grade 12 Biology > Biochemistry > Flashcards

Biochemistry Flashcards

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1
Q

Functions of carbohydrates

A

1) they store energy

2) the are structural

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2
Q

The chemical structure of carbohydrates

A

Carbon:hydrogen:oxygen

1. 2. 1

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3
Q

Types of cerbohydrates

A

Monosaccharides: simple ring sugars, glucose and fructose.

Disaccharides: two monosaccharides combined, sucrose and lactose.

Polysaccharides: polymer(long chains of repeating units) of monosaccharides.

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4
Q

What kids of energy do polysaccharides store?

A

Starch in plants

Glycogen in animals

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5
Q

Polysaccharides

Cellulose

Chitin

A

Polysaccharides are also structural molecules

Cellulose makes up cell wall plants

Chitin makes up exoskeleton, cell walls of fungi

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6
Q

Glucose

A

It is dissolved in water and it is almost always in ring form, but dry. Glucose can have a linear structure.

(Look at photo in notes)

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7
Q

What is the difference of alpha glucose and beta glucose?

A

They are isomers and on alpha glucose on the 4th carbon the hydroxyl group is-on the bottom.

beta glucose on the 4th carbon the hydroxyl group is at the top

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8
Q

Glycoside bonds

A

There are two types of glycoside bonds, Alpha and Beta bonds.

Starch is bonded by 1-4 glycoside bonds. (Image in notes).

Starch is 1-4 linkage of alpha glucose monomers.

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9
Q

Cellulose

A

It is polymer of beta glucose together by beta 1-4 glycoside linkages. (Diagram in notes)

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10
Q

The four major classes of biomolecules!

A

All living things are made up of four classes of biological molecules which are

Carbohydrates

Lipids

Protein

Nucleic acid

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11
Q

Macromolecules

A

They are large molecules composed of thousands covalently bounded atoms.

Molecular structures and functions are inseperated.

They are e

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12
Q

Macromolecules

A

They are large molecules composed of thousands of covalently bonded atoms.

Molecular structures and function are inseperated.

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13
Q

Macromolecules continued

A

They are polymers built from monomers

  • polymer are small building block molecules consisting of many smaller building blocks they are called monomers.
  • three of the four classes of life’s organic molecules are polymers
    • carbohydrates
    • proteins
    • nucleic acid
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14
Q

The synthesis and breakdown of polymers.

A

A dehydration reaction occurs when two monomers bond together through the loss of a water molecule.

Polymers are disassembled to monomers by hydrolysis, a reaction that is essentially the reverse of dehydration reaction.

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15
Q

Dehydration synthesis

A

Dehydration reaction is synthesizing a polymer.

It also removes a water molecule forming a new bond. ( diagrams in notes)

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16
Q

Hydrolysis synthesis

A

This is the breaking down of a polymer.

It also adds a water molecule. ( diagram in notes)

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17
Q

The diversity of polymers

A

Each cell has thousands of different macromolecules.

Macromolecules vary among cells of organisms, they vary a lot between species.

*An immense variety of polymers can be built from a small set of monomers

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18
Q

Carbohydrates serve as fuel and building material

A
  • carbohydrates include sugars and the polymer of sugars
  • monosaccharides are the simplest carbohydrates.
  • carbohydrate macromolecules are polysaccharides, polymers are composed of many sugar building blocks.
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19
Q

Sugars:Monosaccharides

A
  • Monosaccharides have molecular formulas that are usually multiplies of CH2O.
  • Glucose(C6H12O6) is the most common monosaccharide.
  • Monosaccharides are classified by the location of the carbonyl group and the number of carbons in the carbon skeleton.
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20
Q

Sugars:Disaccharides

A
  • A disaccaride is formed when a dehydration reaction joins two monosaccharides.
  • This covalent bond is called a glycosidic linkage.( diagram in notes)
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21
Q

Lipids are Hydrophobic

A

> lipids are the one class of large biological molecules that do not form polymer.

> the unfing feature of lipids is having little or no affinity of water.

> because they consist mostly of hydrocarbons which forms no polar covalent bond they are hydrophobic.

> the most important lipids are fats, steroids, and phospholipids.

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22
Q

Hydrophobic lipids

A

Hydrophobic lipids are composed of c,H,O and are used for insulation and long term energy storage components of cell membrane.

Fats and oils are made up of subunits- glycerol and fatty acids.

> Waxes: mainly used for covering and protection.

> Steroids: precursors to steroid hormones and fat soluble vitamins.

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23
Q

Triglycerides are composed of

A

> Glycerol

- glycerol is a carbon 3 Alcohol
- it has three OH groups attached.

> Fatty acids side chain
- a fatty acid chain of carbon atoms with hydrogen atom

  • at one end of the chain there is carboxyl group, COOH. (Cheek diagram)
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24
Q

Fatty acids composed of

A

> Hydrophobic hydrocarbon chain(tail)
hydrophilic carboxyl acid group(head)

> different fatty acids have different hydrocarbon tails.

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25
Q

Triclycerides

A

An ester link is formed by dehydration synthesis between the glycerol and the fatty acid.

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26
Q

Saturated Fats

A

Contains no double bonds, solid at room temperature.

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27
Q

Unsaturated fat

A

Have double bonds that kink the molecule and they are liquid at room tempurature

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28
Q

Phospholipids

A

Head is hydrophilic and consists of choline,phosphate and glycerol.

> tail is hydrophobic consists of fatty acids.

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29
Q

Fats

A

Fats: are constructed from two types smaller molecules:Glycerol and fatty acids.

> Glycerol is a 3 group carbon alcohol with a hydroxyl group attached to each carbon.

> A fatty acid consists of a carboxyl group attached to a long carbon skeleton. (Check diagram)

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30
Q

Dehydration RXN :add a fatty acid

A

> next add a fatty acid through a dehydration synthesis reaction

> the C double bond O, single bond OH makes it an acid.

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31
Q

Dehydration RXN 2

A

> add a second fatty acid through dehydration synthesis reaction

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32
Q

Dehydration reaction three

A

> the joining of the C of the fatty acid of the O of the hydroxyl group of the glycerol is called and ester linkage. (Check diagram)

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33
Q

Fats are insoluble in swipes enviorments

A

Fats separate from water because Water molecules from hydrogen bonds with each other and exclude fats

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34
Q

Saturated or unsaturated

A

Fats made from saturated fatty acids are called saturated fats and are solid at room temperature.

Most animal fats are saturated

Saturated fatty acids have the maximum number of hydrogen atoms possible and no double bonds.

Check diagram

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35
Q

Unsaturated fats

A

Fats made from unsaturated fatty acids are called unsaturated fats they are liquid at room temperature.

Plant fats and fish fats are usually unsaturated.

They have one or more double bonds.

A rich diet in saturated fat may lead to cardiovascular diseases.

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36
Q

Hydrogenation

A

It is the process of converting unsaturated fats to saturated fats by adding a hydrogen

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37
Q

Trans fat

A

Hydrogenating vegetable oils also creates unsaturated fats with trans double bonds.

These trans fats may contribute more than saturated fats to cardiovascular disease

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38
Q

Fats Function

A

The major function of fats is to store energy

Humans and other mamas store their fat in adipose cells.

Adipose tissue also contains vital organs and insulates the body.

39
Q

Phospholipids

A

When they are added to water they self assemble into bilayer with hydrophobic tails pointing towards inside.

The structure of phospholipids result in bilayer arrangement found in cell membranes.

40
Q

Steroids

A

They are lipids characterized by carbon skeleton consisting of four fused rings.

Cholesterol an important steroid is a component in animal cell membrane.

41
Q

Amino acids

A

All proteins are made up of the same 22 amino acids .

10 amino acids are considered essential (obtained by food)

12 considered non essential(made up by the body)

42
Q

Formation of the peptide bond

A

Two amino acid molecules : the position of the r groups determines the amino acid.

The molecule must be oriented so that the carbolic acid group of one can react with the amino group.

The petite bond forms with the elimination of water molecule, it is another example of condensation reaction.

43
Q

Protein structure (primary)

A

Sequence of amino acid (form a polypeptide chain)

44
Q

Secondary structure of protein

A

Protein chain folds to maximum intermolecular bonding

H bonds are the main force in stabilizing structures

May form alpha helix structure or beta pleated sheets.

45
Q

Tertiary structure of protein

A

Example is a myoglobin a globular protein

Polarity of amino acid is important in how proteins fold.

46
Q

Quadternary structure of protein

A

In protein that contain more than one protein chain refers to interaction between.

47
Q

Prosthetic group

A

Non protein component essential for function

Example hemoglobin

Heme group containing iron is required to bind O2

48
Q

Enzymes

A

They are molecules that catalyze or speed up the biochemical reactions in living things

Three rules to be an enzyme

Most are proteins

Lower the energy of activation requires for a reaction to occur.

Are not consumed by the reaction
49
Q

Catalyst

A

They increase the rate of the chemical reaction by lowering the activation energy.

50
Q

Activation energy ( the energy input required to initiate a chemical reaction)

A

Enzymes interact with substrates

Binding of the enzyme to a substandard cause the enzyme to change shape producing a better induced fit between molecules.

51
Q

Substrates

A

They are molecules that will undergo a reaction when bound to the enzyme

Enzymes will only interact with specific substrates

The substrate fits into the active site.

The substrate binding causes the enzyme to change shape.

Chainring the shape of an enzyme affects its ability to function.

52
Q

Enzyme naming convention

A

The first part of an enzyme usually describes the substrate.

The second part of an enzyme usually indicates the type of reaction it will catalyze

Most enzyme names end in suffix - ase

53
Q

How enzymes work

A

Enzymes makes it easier for chemical reactions to occur

  • by destabilizing the bonds in the substrate
  • by bringing substrates together so they react
  • by decreasing entropy disorder in the system

They make the chemical reactions possible in the cells enviorment

54
Q

How enzymes work continued

A

Through enzymes cells can carry out anabolic and catabolic reactions and end up with a net profit of energy

Cellular respiration is the process of breaking down glucose and storing the energy excess energy from molecule into a form of energy that is useful for the cell

55
Q

Cells use enzymes to process energy and matter

A

Reaction that break chemical bonds release their thermal potential energy.
Ex:burning wood

Organisms obtain energy through enzyme catalyze biochemical reactions.

56
Q

Coenzymes and cofactors

A

Many enzymes require special molecule to help them function correctly.

57
Q

Cofactors

A

In organic molecules ions, such as zinc and iron

58
Q

Coenzymes

A

Organic molecules

Vitamins are prosecutors for many coenzyme

Vitamins must be Aquarius from diet,cells cannot make them.

59
Q

The role of coenzymes

A

ADase oxidizes alcohol

Alcohol cannot be oxidized unless something else is reduced.

60
Q

The environment affects enzyme functions

A

The rate at which an enzyme can bind to a substrate is called the turnover number

Each enzyme has ideal conditions that includes

Tempurature
PH
Substrate concentration
Regulatory molecules

61
Q

Temprature

A

Tempurature has two effects on enzymes
Changes the rate of molecule motion

  • increasing temperature-increases molecular motion and the turnover number.
  • decreasing temperature decreases the molecules motion.
62
Q

Temperature comtinued

A

The second change is that it causes changes in the shape of an enzyme

  • temperature changes above optimum will denature the enzyme
  • this changes it’s shape and it can no longer bind to the substrate and catalyze the reaction.
63
Q

PH

A

In a basic enviorments- lots of OH

  • the acidic side chains could donate protons which affects the charge of the side chain

In and acidic enviorment

  • the basic side chain could accept protons which affects The charge of the side chain
  • a neutral side chain that accepts protons would become positively charged.
  • A neutral side chain that donates protons would become negatively charged.
64
Q

Enzymes

A

Enzymes work together in chains of reactions known as biochemical or metabolic pathways.

> Biochemical pathways are a series of reactions in which the product of one reaction becomes the substrate of the next reaction.

65
Q

Metabolic pathway

A

They are series of chemical reactions carried out by separate enzymes.

It is sequence of chemical reaction, where each reaction is controlled by a separate enzyme.

The product of one enzyme serves as the substrate for the enzyme of subsequent reaction in the metabolic pathway.

66
Q

Enzymes

A

These  bio chemical pathways offer
certain advantages

1) product of the reaction can be directly delivered to the next enzyme
2) The possibility of another one to the side reaction is eliminated
3) all of the reactions can be regulated

67
Q

Enzyme regulation

A

Inhibitors are molecules that bind to an enzyme to decrease enzyme activity.

Competitive inhibitor’s compete with substrates For binding to the same Active site.

Non-competitive inhibitors bind to site other than the enzymes active site

68
Q

Competitive inhibition

A

Competitive inhibitor‘s closely resemble the substrate and they bind into the active site of the enzyme and block the substrate from binding.


69
Q

enzyme regulation

A

Allosteric enzymes exit in either in active or inactive site

Allosteric inhibitor’s bind to Allosteric site to inactive the enzyme

70
Q

Noncompetitive inhibitation

A

Non-competitive because the non-competitive inhibitor does not compete with the substrate binds to the active site

71
Q

DNE

A

Deoxyribonucleic acid carries the genetic instructions used in development functioning and reproduction of all organisms and some viruse

72
Q

RNA

A

Ribonucleic acid

Three types of RNA are involved in converting DNA code into polypeptides

In addition RNA may:

Act as a catalyst like enzyme

Have complex regulatory rules in cells such as regulating gene expression modifying RNA.

73
Q

Structure

A

Consists of

Sugar

Nitrogenous base

Phosphate group

74
Q

The sugars

A

Sugars has 5c sugars

DNA has deoxyribose

RNA has ribose

Bonds to phosphate at group 3 carbon and 5carbon

Bonds to nitrogenous base at 1 carbon
(Check diagram)

75
Q

Nitrogenous base

A

DNA has 4 bases

Adenine that hydrogen bonds to thymine.

Guanine that hydrogen bonds to cytosine.

RNA 4 bases
Unicoloured replaces thymine



76
Q

How to tell the nitrogenous bases apart

A

Guanine and adenine have double ring structure

Thymine and cytosine have single ring structure

They all have phosphate groups

Adenine amino group double ring

Cytosine single ring with amino group

Thymine single ring with oxygen

Guanine double ring with oxygen.

77
Q

DNA Anti-parallel strands

A

Two strands are parallel battle run in opposite directions

One strand runs 5 carbon to 3 carbon other runs 3 carbon to 5 carbon.

5 carbon sugar bonds to phosphate

3 hydroxyl group on sugar

DNA can be single stranded but this is most stable when double-stranded and twisted to 3D helix. 

78
Q

Packaging DNA

A

In eukaryotes DNA It’s wrapped around proteins called histones a coiled form called cremation.

Structure is further compressed by supercooling FaceTime contacted Structure forms chromosomes.

Most prokaryotes lack histones but have supercoiled forms ofDNA held together by special protein.

79
Q

RNA structure

A

RNA is single-stranded

By folding it can form secondary structures that are stabilized by H bonds between nitrogenous base

80
Q

cell membrane function

A

It is semi permeable which means it allows certain materials in and out of the cell

81
Q

Cell transplant

A

The movement of materials in and out of cells can be passive or active.

Passive transport does not require energy

Active transport requires energy

82
Q

Passive transport

A

It is the movement of materials from high to low concentration

With the concentration gradient

83
Q

Active transport

A

Movement of materials from low to high concentration

Against the concentration gradient

84
Q

Passive transport diffusion

A

Diffusion is the movement of small particles from high to low until equilibrium is reached

85
Q

Passive transport osmosis

A

Osmosis is the diffusion of water across a selectively permeable membrane

Water will travel from high to low concentration

What are you doing in route of cells when they are placed in various solutions

Isotonic solutions - equal amount of solute in and out of the cell and the water move in and out in equal amount.

Diesel sounds does not change

86
Q

Facilitated diffusion

A

Diffusion of large Molecules which must be helped through the membrane by travelling through channel proteins and carrier protein
( diagram)

87
Q

Endocytosis

A

The movement of large molecules into the cell from low to high

Requires energy

Molecules bump into cell membrane

Cell membrane wraps around and engulfs particles.

Can you use a temporary vacuole for transport

88
Q

Exocytosis

A

The movement of large molecules out of the cell from low to high concentration and it requires energy.
The golgi body plays a major role in the secreation of proteins and other material through exocytosis.

89
Q

Active transport

A

Active transport is a carrier mediated transport where in molecules and ions Are moved against their concentration gradient across a membrane and requires energy.

90
Q

Primary active transport

A

The energy is derived directly from breakdown of adenosine triphosphate or from other high energy phosphate compound.



91
Q

Secondary active transport

A

The energy is derived from energy stored in the form of an ion concentration gradient between two sides of a cell membrane created originally by primary active transport.

92
Q

Carier protein

A

An active transport carrier protein works differently from the carrier in facilitated diffusion because it is capable of importing energy to the transported substances to move it against the electro chemical gradient by acting as an enzyme in breaking down ATP itself

93
Q

Primary active transport

A

In primary active transport energy in the ATP is required to change the affinity of the carrier proteins binding site when it is exposed and opposite sides of the plasma membrane

The carrier protein also acts as an enzyme that has ATPase activity which means it splits the terminal phosphate from an ATP molecule to yield ADP and inorganic phosphate plus free energy.

Check N a - k pump

94
Q

Secondary active transport

A

This is also called coupled transport. in secondary active transport the downhillflow of of ion is linked to the uphill movement of a second solute either in the same direction as the ion oh in the opposite direction of the ion.
Check diagram

Grade 12 Biology (5 decks)

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