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DAT Bio > Section 1: Chemistry > Flashcards

Section 1: Chemistry Flashcards

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Biology 101 flashcards
1
Q

What are atoms made up of?

A

Neutrons, Protons, and electrons

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2
Q

2 or more atoms held together by chemical bonds are called…

A

Molecules

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3
Q

Chemical bonds result from ____ interactions

A

electron

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4
Q

This is the ability of an atom to attract electrons

A

Electronegativity

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5
Q

What are the 3 bonds types?

A

Ionic
Covalent (polar and non-polar)
Hydrogen

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6
Q

This type of bond is a transfer of electrons from one atom to another due to different electronegativities

A

Ionic bond

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7
Q

This type of bond is the sharing of electrons between atoms with similar electronegativites

A

Covalent

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8
Q

This type of covalent bond is the equal sharing of electrons (identical electronegativites)

This type is the unequal sharing of electrons due to different electronegativities that forms a dipole

A

Nonpolar

Polar

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9
Q

This type of bond is a weak bond between molecules with a hydrogen attached to a highly electronegative atom while also attracted to a negative charge on another molecule (F,O,N)

A

Hydrogen bond

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10
Q

What are the 5 qualities of water?

A 
Excellent solvent
High heat capacity
Ice floats
Cohesion/surface tension
Adhesion
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11
Q

This quality of water results from dipoles of H2O being able to break up charged IONIC molecules

A

Excellent solvent

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12
Q

This is defined as the degree in which a substance changes temperature in response to gain/loss of heat

The temperature of large water bodies are very stable in response to temperature changes of surrounding air, a large amount of energy is required to warm up water. So it has a….

It also has a high heat of _____

A

Heat capacity

High heat capacity

Vaporization

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13
Q

This quality of water results from water expanding as it freezes, becoming less dense then it’s liquid form.

H bonds become rigid and form a crystal that keeps molecules separated

A

Ice floats

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14
Q

This quality of water results from attraction between LIKE substances due to H-bonds; the strong cohesion between H2O molecules produces a high…

A

cohesion/surface tension

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15
Q

This quality of water is due to attraction to unlike substances; capillary action; ability of liquid to flow without external forces (like against gravity)

A

Adhesion

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16
Q

Organic molecules have what atoms?

Macromolecules form _____ which form ______

A

Carbon

Monomers which form polymers

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17
Q

How many of carbon’s 6 electrons are available to form bonds with other atoms?

A

4

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18
Q

This functional group of organic molecules is polar and hydrophilic

A

hydroxyl (OH)

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19
Q

This functional group of organic molecules is polar, hydrophilic, and is a weak acid

A

carboxyl (COOH)

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20
Q

This functional group of organic molecules is polar, hydrophilic, and a weak base

A

NH2

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21
Q

This functional group is polar, hydrophilic, and are present in acidic molecules

A

Phosphate (-PO3)

H3PO4, etc

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22
Q

This functional group of organic molecules is polar and hydrophilic. It can be an aldehyde or ketone

A

Carbonyl

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23
Q

This functional group of organic molecules is nonpolar and hydrophobic

A

Methyl (CH3)

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24
Q

This type of biochemical structure forms monosaccharides, disaccharides, and polysaccharides

A

Carbohydrates

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25
Q

This type of carbohydrate is an alpha or beta sugar molecule base on position of anomeric carbon

An OH pointing up is ____

An OH pointing down is ____

A

Beta

Alpha

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26
Q

This type of carbohydrate is two sugar molecules joined by a glycosidic linkage

A

Disaccharide

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27
Q

What type of linkage occurs between saccharide molecules?

What type of reaction creates this bond?

A

Glycosidic

Dehydration

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28
Q

This type of carbohydrate is a series of connected monosaccharides

They are joined by what type of synthesis?

They are broken down by….

A

Polysaccharides

Dehydration (loss of water from reacting molecules, forms a water molecule)

Hydrolysis (water is used and added to molecules)

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29
Q

This type of carbohydrate is a polymer of α-glucose molecules

Where does it store energy?

A

Starch

Plant cells

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30
Q

This type of carbohydrate is a polymer of α-glucose molecules, but is stored in animal molecules

How is it different from starch?

A

Glycogen

Polymer branching. Starch is branched every 30 residues and glycogen is branched every 8-12 residues

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31
Q

This carbohydrate is a polymer of β-glucose; structural molecule for walls of plant cells and wood

A

Cellulose

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32
Q

This type of carbohydrate is a polymer of β-glucose, but each one has a nitrogen containing group attached to a ring.

A

Chitin

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33
Q

Where is chitin used as a structural molecule?

A

Fungal cell walls and exoskeleton of insects

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34
Q

This type of biochemical molecule is hydrophobic

Used for insulation, energy storage, structural in membrane, and endocrine system (hormones)

A

Lipids

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35
Q

This is three fatty acid chains attached to a glycerol backbone

A

Triglycerides (triacylglycerols)

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36
Q

This type of triglyceride, or fatty acid, has no double bonds

This type of triglyceride or fatty acid has double bonds

A

Saturated fatty acid

Unsaturated fatty acid

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37
Q

Which have a higher boiling point, unsaturated or saturated fatty acids?

Why?

A

Saturated

They stack more tightly(densely). They form plaques which is why they are considered unhealthy

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38
Q

This biochemical molecule is a lipid derivative of two fatty acids and a phosphate group attached to a glycerol back bone

What term describes their hydrophobic/hydrophilic tendencies?

A

Phospholipid

Ampiphatic (both hydrophilic and hydrophobic = membrane bilayer)

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39
Q

This biochemical molecule is a lipid derivative of three 6 membered rings and on 5 membered ring, form hormones and cholesterol

A

Steroids

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40
Q

This lipid derivative is an ester of long chain fatty acids and monohydroxylic alcohols. It is used as protective coating or exoskeleton

A

waxes

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41
Q

These lipid derivatives are fatty acid carbon chains with conjugated double bonds and six membered rings at each ends

A

Carotenoids

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42
Q

This lipid derivative produces colors in plants and animals

A

Carotenoids (carotenes and xanthophylls)

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43
Q

These lipids are 4 joined pyrole rings. Often complexed with a metal, like heme and iron in Hb, chlorphyll with Mg)

A

Porphyrins (tetrapyroles)

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44
Q

You should probably review what all those lipid structures look like and quiz yourself!

A

You know you want to.

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45
Q

Specialized fat cells whose cytoplasm contains nothing but triglycerides

A

Adipocytes

46
Q

These are similar to phospholipids but have a carbon group instead of a phosphate group

A

Glycolipids

47
Q

Lipids are SOLUBLE/INSOLUBLE

A

insoluble

48
Q

Since lipids are insoluble, how are they transported in the blood?

A

Lipoproteins

49
Q

This structure is a lipid core surrounded by phospholipids and apolipoproteins

A

Lipoproteins (used to transport lipids in the blood)

50
Q

Cell membranes need to maintain a certain degree of ______ and are capable of changing fatty acid composition to do so

A

Fluidity

51
Q

In cold weather, to avoid rigidity, cells incorporate more mono and __________ fatty acids into the membrane as they have lower melting points and are more kinked to increase fluidity

In warm weather climates, cells show the opposite trend

A

Polyunsaturated fatty acids

52
Q

Which has a higher boiling point, unsaturated or saturated fatty acids?

Which has a lower melting point?

A

Unsaturated have higher boiling point

Unsaturated have lower melting point

Tricky business!

53
Q

Explain why unsaturated fatty acids have a higher boiling point but a lower melting point

A

Double bonds increase bond polarity

But a more kinked structure leads to less dense packing

54
Q

What is the structure of amino acids?

A

hydrogen group, amine group, carboxyl group, and a variable R group

55
Q

What is the storage protein in milk?

A

Casein

56
Q

What is the storage protein in egg whites?

A

ovalbumin

57
Q

What is the storage protein in corn seeds?

A

Zein

58
Q

This is the transport protein which carries oxygen around the body

A

Hemoglobin

59
Q

These are the transport proteins which carry electrons around the body

A

Cytochromes

60
Q

Does ATP contain ribose or deoxyribose?

A

Ribose!

61
Q

What enzyme catalyzes the reaction that breaks the the α-glycosidic bonds in starch?

A

Amylase

62
Q

These catalyze reaction in both the forward and reverse direction based upon [substrate] (the concentration of substrate)

A

Enzymes

63
Q

What determines an enzyme’s efficiency?

A

Temperature and pH

64
Q

Do enzymes change the spontaneity of a reaction?

A

No!

65
Q

Enzymes are almost always considered to be proteins, but what else can act as an enzyme?

A

RNA (a nucleic acid)

66
Q

These are NON PROTEIN molecules that assist enzymes

A

Cofactors

67
Q

This is the term for the unioned cofactor and the enzyme

What is the term for when the protein is not combined with its cofactor?

A

Holoenzyme

Apoenzyme/apoprotein

68
Q

Can cofactors be both organic and inorganic?

A

Yes

69
Q

These are organic cofactors

These are inorganic cofactors

A

Coenzymes

Metal ions

70
Q

What is it called when a cofactor strongly bonds to an enzyme?

A

Prosthetic Group

71
Q

This classification of protein structure is one made entirely of AAs

This classification are functional and act as carriers or enzymes

These are fibrous, structural (like collagen)

These are made of a simple protein and nonprotein

A

Simple

Albumins and Globulins

Schleroproteins

Conjugated

72
Q

This type of protein is bound to a lipid

This type of protein is bound to a carbohydrate

This type of protein is bound to a pigmented molecule

This type of protein is complexed around a metal ion

This type of protein contains a histone or protamine, is bound to nucleic acid

A

Lipoprotein

Mucoprotein

Chromoprotein

Metalloprotein

Nucleoprotein

73
Q

This is the structure of proteins that is the sequence of AAs

A

Primary structure

74
Q

This is the structure of proteins that is the 3d shape due to H-bonding between amino and carboxyl groups of adjacent amino acids

A

Secondary structure (Alpha helix, beta sheet)

75
Q

This is the structure of proteins that is the 3d structure due to noncovalent interactions between amino acid R groups (subunit interactions)

A

Tertiary structure

76
Q

What are the interactions between R chains that can cause tertiary structure to form?

A 
H bonding
Ionic Bonding
Hydrophobic Interactions
Disulfide Bonds
Van der waals
77
Q

All proteins have a primary structure, and most have a secondary structure. Larger proteins can have a tertiary and quarternary structure. Of these proteins, there are two main broad categories:

A

Globular and Fibrous

78
Q

This category of proteins is somewhat water soluble, has many fxns: enzymes, hormones, membrane pumps/channels/receptors, inter and intracellular storage and transport, osmotic regulation, immune response, etc

A

Globular Proteins

79
Q

This category of proteins is not water soluble, made from long polymers, maintain + add strength to cellular and matrix structure

A

Fibrous proteins

80
Q

_____ proteins are mostly comprised of secondary structure

_____ proteins are mostly comprised of tertiary structure

A

Fibrous

Globular

81
Q

DNA is a polymer of ______

A

nucleotides

82
Q

What are the parts of a nucleotide?

A

Nitrogen base, five carbon sugar deoxyribose, and a phosphate group

83
Q

What are the purines?

What are the pyrimidines?

A

Adenine, guanine = purines

cytosine, thymine = pyrdimidines

84
Q

Which nitrogen base pair has 3 H-bonds?

Which has two?

A

C-G

A-T

85
Q

What is the name for a nucleic acid structure which is only comprised of a sugar and nitrogen base?

A

nucleoside

86
Q

DNA is comprised of two ANTIPARALLEL/PARALLEL strands of a double helix

A

Antiparallel

87
Q

RNA is a polymer of nucleotides that contain ___, not ____

What nitrogen base is replaced by uracil in RNA?

A

ribose, not deoxyribose

Thymine (pairs with adenine)

88
Q

Is RNA usually single or double stranded

A

RNA is usually single stranded

89
Q

What are the 4 principles of cell doctrine/theory?

A
  1. All living organisms are composed of one or more cells.
  2. The cell is the basic unit of structure, function, and
    organization in all organisms.
  3. All cells come from preexisting, living cells. 4. Cells carry hereditary information
90
Q 
This theory proposes that self-replicating ribonucleic acid (RNA) molecules were precursors to current life (based on
deoxyribonucleic acid (DNA), RNA and proteins).
A

RNA world hypothesis

91
Q

RNA STORES GENETIC INFORMATION like DNA and CATALYZES CHEMICAL REACTIONS like an ENZYME protein, so it may have played a major step in the evolution of cellular life.

RNA is unstable STABLE/UNSTABLE compared to DNA, so more likely to
participate in chemical rxns (due to its extra hydroxyl group).

A

RNA world hypothesis

RNA is unstable compared to DNA, due to its hydroxyl group, so it is more likely to participate in chemical reactions

92
Q

What is the central dogma of genetics?

A

iological information cannot be transferred back from protein to either protein or nucleic acid;

DNA ->RNA -> proteins

93
Q

Which type of microscopy is basic, the phase contrast doesn’t kill or stain tissue?

A

Light microscopy

94
Q

This type of microscopy is high magnification and resolution but kills tissue (scanning and magnification)

A

Electron Microscopes

95
Q

This type of microscopy is used to observe chromosomes during mitosis

A

Fluorescence microscopy

96
Q

Centrifugation spins and separates liquified cell homogenates into layers based upon

Which layer is the most dense?

What’s next?

What’s next?

A

Density

Nuclei Layer

Mitochondria

Ribosomes

97
Q

How do catalysts accelerate the rate of a rxn?

A

They lower the activation energy

98
Q

Metabolism =

A

catabolism + anabolism + energy transfer

99
Q

Concentration of ___ and _____ determines which way a rxn will go

A

Reactants and products

100
Q

When the rate of forward and reverse rxns is the same, there is 0 net production, and the reaction is in

A

Equilibrium

101
Q

Enzymes are ___ proteins that act as catalysts

They are specific for what?

Do enzymes change after a reaction?

Do they only catalyze reactions in the forward direction?

Where do substrates bind enzymes? What occurs?

A

Globular

Substrate

No.

No, both forward and reverse

The substrates binds at the active site. Induced fit occurs.

102
Q

Cofactors are nonprotein molecules that assist enzymes usually by donating or accepting some component of a
rxn like….

These are organic cofactors that usually donate or accept electrons

A

electrons

Coenzymes

103
Q

Are vitamins coenzymes or metallic ions?

Inorganic cofactors are usually _____

If metal ions bind covalently, it becomes a

A

Coenzymes

metal ions

Prosthetic group

104
Q

This is a common source of activation energy

How is new ATP formed (what reaction)?

A

ATP

Phosphorylation

105
Q

ATP is formed from _______ + phosphate using energy from an energy rich molecule like _____

A

ADP

Glucose

106
Q

Is ATP potential energy?

A

No, but it contains potential energy

107
Q

These are enzymes that have both an active site for substrate binding and an allosteric site for the binding of an allosteric effector (activator or inhibitor)

A

Allosteric Enzymes

108
Q

This is a substance that mimics the substrate and thereby inhibits the enzyme by binding the active site.

It’s effects can be overcome by

A

Competitive Inhibitor

Increased substrate concentration

109
Q

What changes with competitive enzymes?

A

Kmax is increased, Vmax is unaffected

110
Q

This is a substance that inhibits enzyme binding by binding elsewhere than the active site of an enzyme, the substrate can still bind.

A

Noncompetitive Inhibition

111
Q

What changes in noncompetitive inhibition?

A

Km is unchanged, Vmax decreases

112
Q

This is the property of enzymes where the enzyme becomes more receptive to additional substrate molecules after one substrate molecule attaches to an active site

What class of structures is this usually seen in?

What was the example in class?

A

Cooperativity

Quaternary - enzymes with multiple subunits that each have an active site

Hemoglobin (NOT myoglobin)

DAT Bio (18 decks)

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