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Biology > BIO Ch. 1 > Flashcards

BIO Ch. 1 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Matter

A

Anything that takes up space and has mass

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2
Q

Element

A

A pure substance that has specific physical/chemical properties and can’t be broken down into a simpler substance

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3
Q

Atom

A

The smallest unit of matter that still retains the chemical properties of the element

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4
Q

Molecule

A

Two or more atoms joined together

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5
Q

Intramolecular forces

A

Attractive forces that act on atoms WITHIN a molecule

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6
Q

Intermolecular forces

A

Forces that exist BETWEEN molecules and affect physical properties of the substance (boiling point, melting point, density, etc.)

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7
Q

Monomers

A

Single molecules that can potentially polymerize

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8
Q

Polymers

A

Substances made up of many monomers joined together in chains

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9
Q

Organic molecules

A

Molecules made up of carbon atoms that tend to bond with hydrogen, oxygen, nitrogen

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10
Q

Carbohydrates

A

Contain C,H, and O atoms

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11
Q

Monosaccarides

A

Carbohydrate monomers with empirical formula of (CH2O)n. “n” represents the number of carbons

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12
Q

Ribose

A

5-carbon monosaccaride

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13
Q

Fructose

A

6-carbon monosaccharide

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14
Q

Glucose

A

6-carbon monosaccharide

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15
Q

Isomers

A

Same chemical formula, different arrangement of atoms (e.g. glucose and fructose)

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16
Q

Disaccharides

A

Two monosaccharides joined together by a glycosidic bond (result of dehydration (condensation) reaction)

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17
Q

Dehydration (condensation) reaction

A

A water molecule leaves and a covalent bond forms

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18
Q

Hydrolysis reaction

A

A covalent bond is broken by addition of water

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19
Q

Sucrose

A

Disaccharide made of glucose + fructose

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20
Q

Lactose

A

Disaccharide made of galactose + glucose

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21
Q

Maltose

A

Disaccharide made of glucose + glucose

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22
Q

Polysaccharides

A

Multiple monosaccharides connected by glycosidic bonds to form long polymers

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23
Q

Starch

A

An alpha-1,6 bonded polysaccharide form of energy STORAGE for plants. Linear starch is called amylose; the branched form is amylopectin

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24
Q

Amylose

A

Linear starch

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25
Q

Amylopectin

A

Branched starch

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26
Q

Glycogen

A

An alpha-1,4 bonded polysaccharide form of energy STORAGE for humans. (Much more branching than starch).

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27
Q

Glucans

A

The most abundant polysaccharides in the cell walls of fungi

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28
Q

Cellulose

A

A beta bonded polysaccharide that is a STRUCTURAL component in plant cell walls. Linear strands packed rigidly in parallel

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29
Q

Chitin

A

A beta bonded polysaccharide with nitrogen added to each monomer. It is a STRUCTURAL component in fungi cell walls and insect exoskeletons.

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30
Q

Alpha vs Beta Polysaccharides

A

Alpha: OH group points down in ring structure

Beta: OH group points up in ring structure

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31
Q

Proteins

A

Contain C,H, O and N atoms which combine to form amino acids that link together to build polypeptides (or proteins).

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32
Q

Proteome

A

All the proteins expressed by one type of cell under one set of conditions

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33
Q

Amino acids (a.a.)

A

The monomers of proteins. (Structure is carbon bonded to Hydrogen, amino (NH3+), carboxyl (CO2) and R-group (variant). There are 20 different kinds of amino acids, each with a different “R-group”

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34
Q

Polypeptides (joining and breaking)

A

Polymers of amino acids joined by peptide bonds through dehydration (condensation) reactions). Hydrolysis reactions break peptide bonds. Polypeptide becomes an amino acid chain that contains two end terminals on opposite sides.

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35
Q

N (amino) terminus

A

Side of polypeptide that ends with last amino acid’s amino group

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36
Q

C (carboxyl) terminus

A

Side of polypeptide that ends with the last amino acid’s carboxyl group

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37
Q

Primary protein structure

A

Sequence of amino acids

38
Q

Secondary protein structure

A

Intermolecular forces between the polypeptide BACKBONE (not R-groups) due to hydrogen bonding between the carbonyl (C=O and amino (NH2) groups. Forms alpha-helices or Beta-pleated sheets

39
Q

Transition state

A

Unstable conformation between reactant and products

40
Q

Disulfide bonds

A

A tertiary protein structure created by covalent bonding between the R-groups of 2 CYSTEINE amino acids

41
Q

Quaternary protein structure

A

Multiple polypeptide chains come together to form one protein

42
Q

Protein classification based on STRUCTURE

A

Fibrous, globular or intermediate

43
Q

Tertiary protein structure

A

3-D structure due to interactions BETWEEN R-GROUPS (ionic bonding, H-bonding, dipole-dipole interactions, london dispersion (van der Waal forces). Can create hydrophobic or hydrophilic spaces based on the R-groups. Disulfide bonds are created by covalent bonding between the R-groups of two cysteine amino acids

44
Q

Protein denaturation

A

Loss of protein function and higher order structures. Primary structure remains unaffected.

45
Q

Proteins denature as a result of…

A

High or low temperatures, pH changes, and salt concentrations.

46
Q

Protein functions

A

Storage, hormones, receptors, motion, structure, immunity, enzymes

47
Q

Protein classification based on COMPOSITION

A

Simple (amino acids only) or conjugated (amino acids + other components)

48
Q

Enzymes

A

Act as biological catalysts by binding to substrates (reactants) and converting them into products. Most enzymes are proteins

49
Q

Catalysts

A

INCREASE REACTION RATES by lowering the ACTIVATION ENERGY of a reaction. The TRANSITION STATE is the unstable conformation between reactants and products. Catalysts reduce the energy of the transition state. Catalysts do not shift a chemical reaction or affect spontaneity. (Do not change the net amount of energy a reaction might absorb or release)

50
Q

Hydrogen Bonds

A

Can only occur between H and F,O or N.

51
Q

Active site

A

Enzymes bind substrates at active site which is specific for the substrate that it acts upon. (Active site is located on the enzyme NOT the substrate)

52
Q

Specificity constant

A

Measures how efficient an enzyme is at binding to the substrate and converting it to a product

53
Q

Induced fit theory

A

Describes how the active site molds itself and changes shape to fit the substrate when it binds. The “lock and key” model is an outdated theory of how substrates bind

54
Q

Ribozyme

A

An RNA molecule that can act as an enzyme (a non-protein enzyme)

55
Q

Cofactor

A

A non-protein molecule that helps enzymes perform reactions. A coenzyme is an organic cofactor (i.e. vitamins). Inorganic cofactors are usually metal ions

56
Q

Coenzyme

A

An ORGANIC cofactor (i.e. vitamins). Inorganic cofactors are usually metal ions

57
Q

Holoenzyme

A

Enzymes that are bound to their cofactors

58
Q

Apoenzyme

A

Enzymes that are NOT bound to their cofactors

59
Q

Prosthetic groups

A

Cofactors that are tightly or covalently bonded to their enzymes

60
Q

Protein enzyme denaturation

A

Protein enzymes are susceptible to denaturation. They require optimal temperatures and pH for function.

61
Q

Competitive inhibition

A

Competitive inhibitor competes directly with the substrate for active site binding. The rate of enzyme action can be increased by adding more substrate.

62
Q

Noncompetitive inhibition

A

Noncompetitive inhibitor binds to an allosteric site (a location on an enzyme that is different from the active site) that modifies the active site. In noncompetitive inhibition, the rate of enzyme action CANNOT be increased by adding more substrate.

63
Q

Enzyme Kinetics Plot

A

Used to visualize how inhibitors affect enzymes. The x-axis represents substrate concentration [X] while the y-axis represents reaction rate of velocity (V)

64
Q

Vmax (Enzyme Kinetics Plot)

A

The maximum reaction velocity

65
Q

Michaelis Constants (Km) (Enzyme Kinetics Plot)

A

The substrate concentration [X] at which the velocity (V) is 50% of the maximum reaction velocity (Vmax).
(A small Km implies we only need a little bit of substrate because ability/function is high)

66
Q

Saturation (Enzyme Kinetics Plot)

A

Occurs when all active site are occupied, so the rate of reaction does not increase anymore despite increasing substrate concentration (causes graph plateus)

67
Q

Enzyme Kinetics Plot Competitive Inhibition

A

Km increases, while Vmax stays the same.
(As we add more substrate, the probability that a substrate will occupy the active site over a competitive inhibitor increases. Therefore, the substrate concentration [X] required to reach 50% of Vmax increases, meaning Km increases; however the Vmax is unaffected).

68
Q

Enzyme Kinetics Plot Noncompetitive Inhibition

A

Km stays the same, while Vmax decreases.

(A noncompetitive inhibitor binds to the allosteric site of enzymes, and increasing the substrate concentration [X] will only increase the velocity (V) a certain amount because we CANNOT outcompete allosteric inhibitors. Therefore, Km remains the same because the Vmax decreases, which proportionally decreases the substrate concentration [X] required to reach 50% of the new Vmax).

69
Q

Phosphatase

A

Enzyme cleaves a phosphate group off of a substrate molecule

70
Q

Phosphorylase

A

Enzyme adds a phosphate group to a substrate molecule using inorganic phosphate to break bonds within a substrate

71
Q

Kinase

A

Transfers phosphate group from an ATP molecule to a substrate molecule. Kinases do NOT break bonds in order to add a phosphate group

72
Q

Lipids

A

Contain C, H, and O atoms. Very long hydrocarbon tails that make them very hydrophobic.

73
Q

Triacyglycerol (triglyceride)

A

A lipid molecule with a glycerol backbone (3C + 3OH groups) and t3 fatty acids (long hydrocarbon tails). Glycerol and the 3 fatty acids are connected by ester linkages

74
Q

Saturated Fatty Acids

A

No double bonds and as a result pack tightly (solid at room temperature)

75
Q

Unsaturated fatty acids

A

Have double bonds

76
Q

Monounsaturated fatty acids

A

ONE double bond

77
Q

Polyunsaturated fatty acids

A

TWO or MORE double bonds

78
Q

Cis-unsaturated fatty acids

A

Have KINKS that cause the hydrocarbon tails to bend. Do NOT pack tightly

79
Q

Trans-unsaturated fatty acids

A

Straighter hydrocarbon tails. Pack TIGHTLY

80
Q

Phospholipids

A

Lipid molecules that have a glycerol backbone, one phosphate group and 2 fatty acid tails. Amphipathic because the phosphate group is polar while fatty acids are non-polar. Spontaneously assemble to form lipid bilayers

81
Q

Cholesterol

A

Amphipathic lipid molecule that is a component of the cell membranes. The most common precursor to steroid hormones (lipids have four hydrocarbon rings). Cholesterol is also the starting material for vitamin D and bile acids

82
Q

Factors that influence membrane fluidity

A
  1. Temperature: increased temperatures increase fluidity while decreases temperatures decrease it
  2. Cholesterol: holds membranes together at high temperatures and keeps membranes fluid at low temperatures
  3. Degrees of unsaturation: saturated fatty acids pack more tightly than unsaturated fatty acids, which have double bonds that may introduce kinks
83
Q

Lipoproteins

A

Allow transport of lipid molecules in the bloodstream due to an outercoat of phospholipids, cholesterol, and proteins

84
Q

Low-density lipoproteins (LDLs)

A

“Bad Cholesterol” Low protein density and work to deliver cholesterol to peripheral tissues. Can cause vessel blockage and heart disease

85
Q

High-density lipoproteins (HDLs)

A

“Good Cholesterol” High protein density and take cholesterol away from peripheral tissues and deliver to the liver to make bile. Reduces blood lipid levels.

86
Q

Waxes

A

Simple lipids with long fatty acid chains connected to monohydroxy alcohols (contain a single hydroxyl group) through ester linkages. Used mainly as hydrophobic protective coatings

87
Q

Carotenoids

A

Lipid derivatives containing long carbon chains with conjugated double bonds and six-membered rings at each end. Function mainly as pigments

88
Q

Sphingolipids

A

Have backbone with aliphatic (non-aromatic) amino acids and serve important functions in the plasma membranes of cells.

89
Q

Nucleic acids

A

Contain C, H, O, N and P atoms. Contain nucleotide monomers that build into DNA (deoxyribonucleic acid) and RNA (ribonucleic acid) polymers

90
Q

Nucleosides

A

5-carbon sugar and a nitrogenous base.

91
Q

Nucleotides

A

5 carbon sugar, a nitrogenous base, AND a phosphate group

Biology (1 decks)

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