Biology 20 - Biochemistry, Enzymes, and Digestion (unfinished)

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84 Terms

1

What are macromolecules?

Large, complex, organic molecules

-Includes carbonhydrates, lipids, proteins, and nucleic acids

-Anabolic, macromolecules are all created from smaller subunits

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2

Reasons why water is required in our bodies

-Solvent to dissolve and transports salts, food particles and gases

-Regulates and transports temperatures

-Water increase permeability and improve diffusion rates

-Water cleanses and lubricates body tissues

-Water supports and protects organs

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3

What is organic material structure

Matter that is derived from carbon backbone(carbon chains)

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4

What are inorganic compounds

Compounds that aren’t carbon chain(typically only have one carbon)

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5

What is a polymer

Repeating units that make up macromolecules

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6

What are monomers

Small subunits that connect together to make up polymer

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7

polymerization

Process of joining together many monomers to create a polynomer

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8

What is dehydration synthesis

Anabolic reaction that is done through removing a water molecule to bond molecules together

-Anabolic reactions are endothermic

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9

What is hydrolysis

Adding water to a substance to break apart the molecules. This is a catabolic reaction.

-Catabolic reactions are exothermic

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10

What are carbohydrates?

-Molecules that contain carbon, oxygen, and hydrogen.

-AKA sugars

-Can be classified as simple sugars or starches(polysaaccharides)

-Carbs are energy sources

<p>-Molecules that contain <em>carbon</em>, oxygen, and hydrogen.</p><p>-AKA sugars</p><p>-Can be classified as simple sugars or starches(polysaaccharides)</p><p>-Carbs are energy sources</p>
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11

What are simple sugars

one or two individual sugar units

-monosaccharides

-disaccharides

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12

What are the 3 different categories of carbohydrates

-Monosaccharides

-Disaccharide

-Polysaccharide

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13

What are monosaccharides?

Carbs that contain only one sugar unit, is a simple sugar

-a monomer

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14

disaccharide

carbs that contain only two sugar units, is also a simple sugar

-technically a dinomer

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15

polysaccharides aka starches

Mutiple sugar units(3+ sugar units)

-Made up of many monosaccharides

-Made through dehyration synthesis

Complex sugars

Released in boiling water

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16

What are the two tests for carbohyddrates

-Benedict’s test

-Iodine test

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17

What is a reducing sugaar

glucose/fructose- simple sugar

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18

How does benedicts test work

-Quantitative test that uses benedicts reagent, in which when adding certain compounds within the solution where shift the colour of the solution

-Identifies reducing sugars such as glucose and lactose

-Colour shifts within the solution represent the percent of reducing sugars in the sample

Blue 0%

Light green <0.5%

Greenhish 0.5-1.0%

Yellowish 1.0-1.5%

Orangish red 1.5-2%

Brick red >2%

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19

How does iodine test works

Identifies starches(polysaccharides)

-It is a Qualitative test

Uses iodine to show if starches is present

Yellow-brown shows theres no starches/negative

Blue-black shows theres starches/positive

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20

What determines polysaccharides shape and function

The way they are arranged determines their shape and function

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21

What is glycogen

Carbohydrate that is stored and reserved when needed, because we dont use them at first

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22

Insulin

Proteins that help absorbs carbohydrates within our blood

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23

What happens when your blood sugars become too low

When your blood levels become too low glycogen is released from your liver to even out your blood sugar levels

<p>When your blood levels become too low glycogen is released from your liver to even out your blood sugar levels</p>
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24

What happens when your blood sugars become too high

When your blood levels become too high insulin is released to help cells absorb glucose

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25

What is cellulose?

helps things move;cell wall in plants

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26

What is fiber

Helps release the waste within our body

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27

What are lipids?

Lipids consist of glycerol(3 carbon chain) and fatty acids which varies

-Aka fats or oils

-insoluble in water

<p>Lipids consist of glycerol(3 carbon chain) and fatty acids which varies</p><p>-Aka fats or oils </p><p>-<u>insoluble</u> in water</p>
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28

What are the functions of lipids

-energy storage

-cushions delicate organs

-carries fat soluble vitamins

-makes up sex hormones

-insulation warmth

-increase buoyancy

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29

Different types of lipids

-Triglycerides

-Phosphilipid

-Waxes

-Steroids

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30

Triglycerides

-”true” fats/oils you consume in your diet

-1 glycerol + 3 fatty → 1 triglyceride + 3 H2O

-Dehydration synthesis process since water is released

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31

2 kind of fatty acids

Saturated and Unsaturated

<p>Saturated and Unsaturated </p>
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32

Saturated fatty acids

-Comes from animals, becaus eonly single bonds within chain, MAXIMIZE HYDROGEN

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33

Unsaturated fatty acids

-Usually liquid

-Double bonds

-healthier, and easier to break

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34

Animal triglyceride

-Know as fats

-Solid

-Glycerol + 3 saturated fatty acids

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35

Plants triglyceride

-Know as oils

-Liquid

-Glycerol + 3 unsaturated fatty acids

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36

Phopholipids

-Lipids that make up the lipid bi-layer in the cell membrane

-Unique molecules because they have different properties on each side

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37

Waxes

protective coating feathers. Furs and leaves

They are also formed through dehydration synthesis

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38

Steroids

-Lipids makes up sex hormones as well as good and bad cholesterol

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39

High density lipoprotein(HDL)

Good cholesterol is responsible for reducing your levels of bad cholesterol

-Takes bad cholesterol down to liver to be broken down

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40

Low density lipid(LDL)

It is bad cholesterol and blocks you blood flow

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41

Brown paper bag test

Its a test for lipids

AKA translucent test, if theres light that can penetrate through theres fat(lipids)

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42

Proteins

-Makes up most cellular structures

-Formed from tiny amino acid put together in long chains

<p>-Makes up most cellular structures</p><p>-Formed from tiny amino acid put together in long chains </p>
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43

R group

Varies amino acid, interactions between R groups can cause changes in the shape of a protein(coil or twist)

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44

What are proteins made out of

ELements such as C, H, O, N and sometimes S.

-Proteins are made out of amino acids and peptides

<p>ELements such as C, H, O, N and sometimes S.</p><p>-Proteins are made out of amino acids and peptides</p>
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45

What are proteins

Polynomers made up of monomers called amino acids

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46

what are peptides

Bonds within proteins/polypeptides

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47

Whats a polypeptide

Molecule that has between 3 to 300 amino acids

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48

What are molecules with more than 300 amino acids

Proteins!

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49

How many amino acids can the body synthesize

11 out of the 20 amino acids, these amino acids are called non essential

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50

What are essential amino acids

The other 9 amino acids that come from our diet

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51

What are different actions proteins can undergo

-Denaturation

-Coagulation

-Deamination

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52

What is denaturation

-Temporary change in protein shape caused by addition of heat, pH, or chemicals. Change is reversed when conditions return to normal

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53

What is coagulation

Permanent change in protein shape. Caused by excessive heat, pH, or chemicals. The protein will never resume original shape even when conditions return to normal

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54

What is deamination

Removal of Amino Acids from protein or polypeptide chain. This is a natural action during digestion

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55

Biuret test

Test for proteins, is a qualitative and quantative test but using samples to describe change, which gather

Blue to purple, the bigger the molecule the more protein.

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56

Nucleic acids

Nucleic acid make up DNA and RNA

-They contain phosphate, sugar, and nitrogen base

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57

What are nucleotides

Monomers that make up nucleic acids

-Made up of 5 carbon sugar

-Phosphate

-Nitrgoen containing base

<p>Monomers that make up nucleic acids</p><p>-Made up of 5 carbon sugar</p><p>-Phosphate</p><p>-Nitrgoen containing base</p>
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58

DNA

-Sugar phosphate back bone

-Sequence of bases that makes up the code determining our traits

Bonding

A with T

G with C

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59

What are enzymes

Protein biological catalysts that increase reaction rates by reducing the amount of energy needed to start a reaction.

-Usually ends in an ase suffix

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60

What is activation energy

Energy added at the beginning of a reaction to get reactants to proceed to form products

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61

Homeostatic meaning

Ability to keep internal environment stable; to keep balance; setpoints

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62

What is the homeostatic temperature in our bodies

37 degrees celcius, if the temperature was too high it would cause major biochemical problems that could be fatal.

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63

What does enzyme allow

They allow reactions to take place at lower temperatures at faster rates by reducing the activation energy needed

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64
<p>Analyze data seen in photo</p>

Analyze data seen in photo

An uncatalyzed reaction requires higher activation energy than does a catalyzed reaction

-There is no difference in free energy between both reactions

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65

Enzymes in relation with monomers and polynomers

Enzymes can either bind monomers together or break polynomers down into monomers

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66

How does an enzyme work

Substrate enters active site, subtrate bonds to the active site, water is added or released in order to break apart or bind products. The products are thn released.

There are two theories regarding on how enzymes react

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67

What are the two theories on how enzymes react

“Lock and key” and “induced fit”

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68

What is the lock and key theory for enzymes

Only one enzyme for one shape of subtrate(exact geometry)

-Fits like a puzzle piece

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69

What is the induced fit theory regarding enzymes

Active site alters slightly to fit closely related substrate shapes

-Changes shape slightly to make fit

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70

How does temperature affect enzyme reaction

When temperature will from the homeostatic optimal, enzyme activity will decrease

-Most enzymes in the body(37 degree homeostatic optimal) will denature at 50 degrees ceasing reactions

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71

How does pH affect enzymes

-Most enzymes(within the body) will operate the best at near neutral(pH 7). However enzyme pH preference is dependant on where it is found in the body.

If pH fluctuates too much from the homeostatic optimal enzymes will denature and reduce the turnover number

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72

Turnover number

The efficiency of an enzyme/how many times enzyme can react with substrate to create product

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73

How does enzyme concentration affect enzyme reaction

If the body produces or activates more enzymes, it will increase the turnover number, since the subtrates have a better chance of joining up with an enzyme

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74

How does co enzyme and co factor concentration affect enzyme reaction

If the body has more co-enymes and co factor this improves enzyme reactions, because it allows for the greater ability to re-alter active sites so that new substrates can be wokred on

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75

How does substrate concentration affect enzyme reaction

The more substrate will increase enzyme reaction rate, however works to a certain point(saturation)

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76

Allosteric site

Place on an enzyme that is not the active site

-Substrate may bind with this place HOWEVER will change the shape of an enzyme and influencing its ability to be active

Kind of acts like a switch for the enzyme

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77

Allosteric activity

Action involving the allosteric site

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78

Allosteric activator

When an molecule binds to an activator site which activates the enzyme

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79

Allosteric inhibitor

When a molecule binds with a inhibitor site where the active site is in the incorrect formation

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80

How does product concentration affect enzyme activity

The more products, the less enzymes, the less product the more enzymes. This mechanism allows for the maximum efficiency depending on circumstances. This mechanism of which trying to reach a setpoint is called feedback inhibition(negative feedback)

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81

What is feedback inhibition

A type of negative feedback, which is a corrective mechanism that slows down or stops a process.

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82

What is negative feedback

Process that maintains balance by reducing or counteracting a change

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83

What is competitive inhibitors

Substances that resemble substrates in shape but are not true subtrate. They bind to the active site and prevent true substrates from being worked on

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84

Non-compeitive inhibitors

Substances that bind to the enzyme at a location other than the active siter. This alters the protein shape and indirectly affects the shape of the active site so that true subtrates cannot get on

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