Biology - Ch 1 - The Basis Of Life

Front 1

Metabolism

Back 1

The sum of all chemical reactions that occur in the body.

____________ can be be divided into catabolic and anabolic reactions.

Front 2

Catabolic Reactions

Back 2

Break down large chemicals and release energy.

Front 3

Anabolic Reactions

Back 3

Build up large chemicals and require energy.

Front 4

Ingestion

Back 4

The acquisition of food and other raw materials.

Front 5

Digestion

Back 5

Process of converting food into a usable soluble form so that it can pass through membranes in the digestive tract and enter the body.

Front 6

Absorption

Back 6

Passage of nutrient molecules through the lining of the digestive tract into the body via diffusion or active transport.

Front 7

Transport

Back 7

Circulation of essential compounds required to nourish the tissues, and the removal of waste products from the tissues.

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Assimilation

Back 8

The building up of new tissues from digested food materials.

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Respiration

Back 9

The consumption of oxygen by the body. Cells use oxygen to convert glucose into ATP, a ready source of energy for cellular activities.

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Excretion

Back 10

The removal of waste products produced metabolic processes like respiration and assimilation.

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Synthesis

Back 11

The creation of complex molecules from simple ones (anabolism),

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Regulation

Back 12

The control of physiological activities. The body's metabolism functions to maintain its internal environment in a changing external environment.

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Irritability

Back 13

Ability to respond to a stimulus and is part of regulation.

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Growth

Back 14

Increase in size due to synthesis of new materials.

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Photosynthesis

Back 15

The process by which plants convert CO2 and H2O into carbohydrates.

Sunlight is harnessed by chlorophyll to drive this reaction.

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What are all living things composed of?

Back 16

Carbon, Hydrogen, Oxygen, Nitrogen, Sulfur, Phosphorus. Traces of Magnesium, iodine, iron, calcium.

Front 17

Protoplasm

Back 17

The living substance within a cell. Seperate from the non-living parts.

Front 18

H2O

Back 18

Water

Front 19

CO2

Back 19

Carbon Dioxide

Front 20

C6H12O6

Back 20

Glucose

Front 21

Two divisions of chemical compounds

Back 21

Inorganic and Organic

Front 22

Inorganic Compounds

Back 22

Compounds that do not include the element Carbon including salts and HCl

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Organic Compounds

Back 23

Compounds made by livings systems and contain carbon.

Including carbohydrates, lipids, proteins, and nucleic acids.

Front 24

Ratio of Carbon:Hydrogen:Oxygen in carbohydrates

Back 24

C:H:O
1:2:1

Front 25

What are carbohydrates used for?

Back 25

Storage forms of energy and structural molecules.

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What stores energy in in animals?

Back 26

Glucose and Glycogen

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What stores energy in plants?

Back 27

Starch

Front 28

Monosaccharides

Back 28

Single sugar subunits

Glucose or Fructose

Front 29

D-Fructose

Back 29

CH2OH
|
|=O
HO--|--H
H--|--OH
H--|--OH
|
CH2OH

Front 30

D-Glucose

Back 30

CHO
|
H--|--OH
HO--|--H
H--|--OH
H--|--OH
|
CH2OH

Front 31

D-Galactose

Back 31

CHO
|
H--|--OH
HO--|--H
HO--|--H
H--|--OH
|
CH2OH

Front 32

D-Mannose

Back 32

CHO
|
HO--|--H
HO--|--H
H--|--OH
H--|--OH
|
CH2OH

Front 33

Disaccharide

Back 33

Two monosaccharide subunits joined by dehydration synthesis

Front 34

Dehydration synthesis

Back 34

1-4' addition of two monosaccharides. Loss of OH and H results in loss of H2O

Front 35

Polysaccharides

Back 35

Polymers or chains of repeating monosaccharide subunits.

1-4' addition.

Glycogen and starch are ________ and are insoluble in water.

Front 36

Are polysaccharides insoluble in water.

Back 36

Yes, they are insoluble in water.

Front 37

Hydrolysis

Back 37

Adding water, large polymers can be broken down into smaller subunits.

Front 38

Dehydration

Back 38

Polysaccharides are formed by removing water.

Front 39

What are lipids composed of?

Back 39

C,H,O. Just like carbohydrates.

Three fatty acid molecules bonded to a single glycerol backbone.

Front 40

What is the ratio of atoms in lipids?

Back 40

H:O ratio is much larger than 2:1

Front 41

Why are fatty acids hydrophobic?

Back 41

Long carbon chains.

Front 42

Why are fatty acids acidic?

Back 42

Carboxylic acid group.

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Do lipids form polymers?

Back 43

NO, lipids do not form polymers.

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What are lipids used for?

Back 44

Chief means of food storage in animals.

Release more energy per gram weight than any other class of biological compounds.

Provide insulation and protection against injury since they are a major component of fatty (adipose) tissue.

Front 45

Lipid Derivatives

Back 45

Phospholipids, Waxes, Steroids, Carotenoids, Porphyrins

Front 46

Phopholipids

Back 46

Contain glycerol, two fatty acids, phophate group, nitrogen containing alcohol

Front 47

Waxes

Back 47

Esters of fatty acids and monohydroxylic alcohols.

Found as protective coatings on skin, fur, leaves of higher plants.

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Steroids

Back 48

Three fused cyclohexane rings and one fused cyclopentane ring.

Cholesterol, Sex hormones, corticosteroids.

Front 49

Sex Hormones

Back 49

Testosterone and Estrogen

Front 50

Carotenoids

Back 50

Fatty acid-like carbon chains containing conjugated double bonds and carrying six-membered carbone rings on each end.

Pigments that produce red, yellow, orange, and brown colors in plants and animals.

Two subgroups: Carotenes and Xanthophylls.

Front 51

Porphyrins

Back 51

AKA: Tetrapyrroles

Contain four joined pyrrole ringes

Often complexed with a metal.

Heme complexes with Fe in hemoglobin.

Chlorophyll complexed with Mg.

Front 52

Proteins elements

Back 52

Contains:
Carbon
Hydrogen
Oxygen
Nitrogen
Sometimes:
Phosphorus
Sulfur

Front 53

How are amino acids joined together?

Back 53

Peptide Bonds via dehydration synthesis.

Front 54

What are chains of Amino acids called?

Back 54

Chains of amino acids formed via peptide bonds are called polypeptides or simply peptides.

AKA: Protein

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Protein Primary Structure

Back 55

Sequence of Amino Acids

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Protein Secondary Structure

Back 56

alpha helix coiling or B sheet pleating

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Protein Tertiary Structure

Back 57

Global 3-D structure of Protein

Front 58

Protein Quaternary Structure

Back 58

Structure how multiple proteins fit together

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Structure of Argenine

Back 59

Picture

Front 60

Structure of Lysine

Back 60

Picture

Front 61

Structure of Histidine

Back 61

Picture

Front 62

Simple Proteins

Back 62

Composed entirely of amino acids

Front 63

Albumins and globulins

Back 63

Primarily globular in nature.

Functional proteins that act as carriers or enzymes.

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Scleroproteins

Back 64

Fibrous in nature.

Act as structural proteins.

Collagen is an example.

Front 65

Conjugated Proteins

Back 65

Contain a simple protein portion, plus at least one nonprotein fraction.

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Lipoproteins

Back 66

Protein bound to lipid.

Front 67

Mucoproteins

Back 67

Protein bound to carbohydrate

Front 68

Chromoproteins

Back 68

Protein bound to pigmented molecules

Front 69

Metalloproteins

Back 69

Protein complexed around a metal ion

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Nucleoproteins

Back 70

Protein containing histone or protamine (nuclear protein) bound to nucleic acids

Front 71

Protein Function - Hormones

Back 71

Function as chemical messenger secreted into circulation.

Insulin and ACTH

Front 72

Protein Function - Enzymes

Back 72

Biological catalysts that act by increasing the rate of chemical reactions important for biological functions.

Amylase and lipase and ATPase

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Protein Function - Structural Proteins

Back 73

Contribute to physical support of a cell or tissue.

Extracellular: collagen
Intracellular: proteins in cell membranes.

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Protein Function - Transport proteins

Back 74

These are carriers of important materials.

Hemoglobin carries Oxygen in circulation.

Cytochromes carry electrons during cellular respiration.

Front 75

Protein Function - Antibodies

Back 75

Bind to foreign particles (antigens) including disease-causing organisms, that have entered the body.

Front 76

What are enzymes?

Back 76

Organic catalysts.

Front 77

What is a catalyst?

Back 77

Lower activation energy of a reaction.

Increase the rate of the reaction.

Do not affect the overall ⋀G of reaction.

Are not changed or consumed in the course of the reaction.

Front 78

Why are enzymes needed?

Back 78

All living systems must be continuously controlled.

Enzymes regulate metabolism by speeding up or slowing down certain chemical reactions.

Front 79

How do enzymes work?

Back 79

By decreasing the activation energy.

Front 80

What are enzymes made of?

Back 80

Proteins.

Thousands of of different enzymes can conceivably be formed.

Many enzymes are conjugated proteins and have a non-protein co-enzyme. Both must be present in order for enzymatic activity.

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What is the specificity of an enzyme?

Back 81

Enzymes are very selective.

Catalyze only 1 reaction or 1 specific class of related reactions.

Front 82

Substrate

Back 82

Molecule upon which an enzyme acts.

Front 83

Active Site

Back 83

Area on each enzyme to which the substrate binds.

Front 84

Lock and Key Theory

Back 84

Theory that the spatial structure of an enzyme's active site is exactly complementary to the spatial structure of its substrate.

Two fit together like a lock and key.

This theory is largely discounted.

Front 85

Induced Fit Theory

Back 85

Theory that the active site is flexible.

When appropriate substrate come in contact with the active site, conformation of the active site changes to fit the substrate.

Front 86

Enzyme Reversibility

Back 86

Most enzyme reactions are reversible.

The product synthesized by an enzyme can be desynthesized by the same enzyme.

Front 87

Enzyme Action - Effects of Temperature

Back 87

As temperature increases, in general enzyme activity increases.

At an optimal temperature, heat alters the shape of the protein leading to deactivation of the enzyme and rapid drop in rate.

Front 88

Enzyme Action - Effects of pH

Back 88

For each enzyme, there is optimal pH where activity decreases above and below this pH.

Many human enzymes are max at pH 7.2.

Pepsin works well at pH=2 (acidic) of stomach.

Pancreatic enzymes work best at pH 8.5 (in small intestine)

Front 89

Enzyme Action - Effects of Concentration

Back 89

Concentration of substrate and enzyme greatly effect the rate.

Increasing concentration will increase rate until all active sites are full.

Front 90

Examples of Enzyme Activity - Hydrolysis

Back 90

Hydrolysis functions to digest large molecules into smaller components.

Lactase hydrolyzes lactose to the monosaccharides glucose and galactose.

Proteases degrade proteins to amino acids.

Lipases break down lipids to fatty acids and glycerol.

Front 91

Lactase

Back 91

Hydrolyzes lactose to the monosaccharides glucose and galactose.

Front 92

Proteases

Back 92

Degrade proteins to amino acids.

Front 93

Lipases

Back 93

Lipases break down lipids to fatty acids and glycerol.

Front 94

Examples of Enzyme Activity - Synthesis

Back 94

Reversibility of enzymes.

Forward and Backward directions occur in different locations within the cell.

Front 95

Cofactors/Coenzymes

Back 95

Many enzymes require a non-protein element to become active.

Cofactor - Metal cations
Coenzyme - Organic groups

Most coenzymes are obtained from vitamins, can't be built.

Cofactors that bond to enzyme with strong covalent bond are called prosthetic groups.

Front 96

Prosthetic Groups

Back 96

Cofactors that bond to enzyme with strong covalent bond

Front 97

Nucleic Acids Elements

Back 97

C,H,O,N,P

Front 98

Nucleic Acids

Back 98

Polymers of subunits called nucleotides.

Nucleic acids (DNA,RNA) code all the information required by an organism to produce proteins and replicate.

Front 99

Nucleotide Picture

Back 99

Picture

Front 100

Cell Theory (4)

Back 100

1) All living things are composed of cells.
2) The cell is the basic functional unit of life.
3) Cells arise only from pre-existing cells.
4) Cells carry genetic information in the form of DNA. The genetic material is passed from parent to daugher cell.

Front 101

Microscopy

Back 101

Increase in the apparent size of an object.

Front 102

Resolution

Back 102

Differentiation of two closely situated objects.

Front 103

Total Magnification in compound microscope.

Back 103

Total=Eyepiece*Objective

Front 104

Diaphragm

Back 104

Controls amount of light passing through specimen.

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Coarse adjustment

Back 105

Roughly focuses the image

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Fine adjustment

Back 106

Sharply focuses the image

Front 107

Compound light microscopy

Back 107

Two lense system

In general for non-living

Staining is often used resulting in cell death.

Front 108

Phase contrast microscopy

Back 108

Special type of light microscope that permits study of living cells.

Difference in refractive indexes creates contrast between cellular structures.

Front 109

Electron Microscopy

Back 109

Beam of electrons to allow a thousandfold higher magnification that is possible with light.

Living specimen not possible.

Must be fixed, sectioned, and sometimes stained with solutions of heavy metals.

Front 110

Centrifugation

Back 110

Seperate cells or mixtures without destroying them in the process.

Heavier components will be lower.

Front 111

Organelles

Back 111

Specialized components within the cell (structure and function).

Front 112

In a Nutshell:
Prokaryotes and Eukaryotes

Back 112

Example:
Prokaryotes - Bacteria
Eukaryotes - Protists, fungi, plants, animals

Cell Wall:
Prokaryotes - Present in all, composed of peptidoglycans
Eukaryotes - Cell wall present in fungi and plants only

Nucleus:
Prokaryotes - No Nucleus
Eukaryotes - Nucleus Present

Ribosomes:
Prokaryotes - Subunits=30S&50S
Eukaryotes - Subunits=40S&60S

Organelles:
Prokaryotes - No membrane-bound organelles
Eukaryotes - Membrane-bound organelles

Front 113

Cell Membrane (Plasma Membrane)

Back 113

Encloses Cell

Exhibits selective permeability

Regulates passage in and out of cell

Lipid bilayer leads to permeability for small nonpolar such as oxygen or small polar such as water.

Small charged particles are usually able to cross through protein channels.

Larger charged molecules cross membrane with assistance of carrier proteins.

Front 114

Fluid mosaic model

Back 114

Cell membrane consists of a phospholipid bilayer with proteins embedded throughout.

The lipids and many of the proteins can move freely within the membrane.

Front 115

Nucleus

Back 115

Controls activities of the cell, including cell division.

Surrounded by nuclear membrane.

Contains the DNA, which is complexed with structural proteins called histones, to form chromosomes.

Nucleolus is dense structure in nucleus where ribosomal RNA (rRNA) synthesis occurs.

Front 116

Nucleolus

Back 116

Dense structure in nucleus where ribosomal RNA (rRNA) synthesis occurs.

Front 117

Ribosome

Back 117

Sites of protein production and synthesized by nucleolus.

Free ribosomes found within cytoplasm.

Bound ribosomes line the outer membrane of the endoplasmic reticulum.

Front 118

Endoplasmic Reticulum

Back 118

Network of membrane-enclosed spaces involved in the transport of materials throughout the cell, particularly those materials destined to be secreted by the cell.

Front 119

Golgi Apparatus

Back 119

Receives vesicles and their contents from the smooth ER, modifies them, repackages them into vesicles, and distributes to cell surface via exocytosis.

smooth ER -> modify -> repackage to vesicles -> distributes via exocytosis

Front 120

Mitochondria

Back 120

Sites or aerobic respiration (suppliers of energy)

Bounded by an outer and inner phospholipid bilayer.

Front 121

Cytoplasm

Back 121

Most of cells metabolic activity occurs here.

Transport within cytoplasm occurs by cyclosis.

Front 122

Cyclosis

Back 122

Transport within cytoplasm occurs by cyclosis (streaming movement within the cell).

Front 123

Vacuoles and Vesicles

Back 123

Membrane bound sacs involved in the transport and storage of materials that are ingested, secreted, processed, or digested by the cell.

Vacuoles are larger than vesicles and more likely to be found in plant than in animal cells.

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Centrioles

Back 124

Specialized microtubule involved in spindle organization during cell division and not bound by a membrane.

Animal cells usually have a pair of centrioles that are oriented at right angles to each other and lies in region called centrosome.

Plant cells do no contain centrioles.

Front 125

Lysosome

Back 125

Membrane bound vesicles that contain hydrolytic enzymes involved in intracellular digestion.

Break down material ingested by the cell.

Injured cells can commit suicide by rupture of lysosome membrane releasing hydrolytic enzymes (autolysis)

Front 126

Autolysis

Back 126

Cell suicide

Front 127

Cytoskeleton

Back 127

Composed of microtubules and microfilaments gives cell mechanical support, maintains shape, funtions in cell motility.

Front 128

Plants Cell differences from animal cells

Back 128

No centrosome

Presence of cell wall composed of cellulose

Chloroplasts in many cells of green plants. Sites of snythesis of organic compounds.

No lysosomes.

Many vacuoles. Mature plants usually contain one large vacuole.

Front 129

Transport methods across cell membrane

Back 129

Simple Diffusion

Facilitated Diffusion

Active Transport

Front 130

Simple Diffusion

Back 130

Net movement of dissolved particles down their concentration gradients.

Passive, requires no energy.

Front 131

Osmosis

Back 131

Diffusion of water from a region of lower solute concentration to a region of higher solute concentration.

Front 132

Plasmolysis

Back 132

Cell shrivels due to hypertonic solution

Front 133

Isotonic Solution

Back 133

Cell and solution same solute concentration

Front 134

Hypotonic

Back 134

Cell solute concentration much greater than solution.

Front 135

Hypertonic

Back 135

Solution concentration much greater than cell.

Front 136

Lyse

Back 136

Bursting of cell.

Front 137

Types of Transport in a Nutshell

Back 137

Passive Diffusion:
Down Gradient
No Carrier
No energy required

Facilitated Diffusion:
Down gradient
Carrier
No energy required

Active Transport:
Against gradient
Carrier
Energy required

Front 138

Facilitated diffusion

Back 138

Net movement of dissolved particles down their concentration gradient through special channels or carrier proteins in cell membrane.

Requires no energy.

Front 139

Active transport

Back 139

Net movement of dissolved particles against their concentration gradient with the help of transport proteins.

Requires energy.

Front 140

Intracellular Circulation

Back 140

Brownian Movement - Movement of particles due to kinetic energy which spreads small suspended particles throughout the cyoplasm of the cell.

Cyclosis or Streaming: circular motion of cytoplasm around the cell transport molecules

Endoplasmic reticulum: provides channels throughout the cytoplasm, provides direct continuous passageway from the plasma membrane to the nuclear membrane.