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Biology > Exam 1 > Flashcards

Exam 1 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Peptide Bond

A

The covalent bond (C–N) formed by a condensation reaction between two amino acids; links the residues in peptides and proteins.

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2
Q

Polymerization occurs through…

A

Condensation/dehydration reactions

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3
Q

The components of an amino acid group include…

A

Carboxyl group, hydrogen atom, amino group, r-group, carbon atom

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4
Q

Define a positive control in an experiment

A

Negative-absence of effect

Positive- presence of effect

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5
Q

What is the most abundant material in cells?

A

Water

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6
Q

What are the four types of molecules in cells?

A

Nucleic acids, glycans, proteins, lipids

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7
Q

What is the main form of energy in cells?

A

Glucose

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8
Q

Which type of molecule is most numerous in a cell?

A

Protein

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9
Q

The shorthand notation for carbohydrate…

A

CH2O

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10
Q

What are the two groups of nucleic acids?

A

Nitrogenous base, sugar

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11
Q

Pilli and flagella are examples of what?

A

Glycans

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12
Q

What are the three major types of eukaryotes?

A

Plant, animal, cell

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13
Q

Lysosomes function?

A

Recycle used parts of a cell

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14
Q

Three characteristics of Polypeptides

A
  1. R-groups
  2. Directionality
  3. Flexibility
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15
Q

Condensation/ Dehydration Reaction

A

A chemical reaction in which two molecules are joined covalently with the removal of an –OH from one and an –H from another to form water. Also called a dehydration reaction. Compare with hydrolysis.

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16
Q

Primary Structure of a Protein

A

The sequence of amino acids in a peptide or protein; also the sequence of nucleotides in a nucleic acid. Compare with secondary, tertiary, and quaternary structure.

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17
Q

Secondary structure of a protein

A

In proteins, localized folding of a polypeptide chain into regular structures (e.g., α-helix and α-pleated sheet) stabilized by hydrogen bonding between atoms of the backbone. In nucleic acids, elements of structure (e.g., helices and hairpins) stabilized by hydrogen bonding and other interactions between complementary bases. Compare with primary, tertiary, and quaternary structure.

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18
Q

Tertiary structure of a protein

A

The overall three-dimensional shape of a single polypeptide chain, resulting from multiple interactions among the amino acid side chains and the peptide backbone. Compare with primary, secondary, and quaternary structure.

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19
Q

quaternary structure of a protein

A

The overall three-dimensional shape of a protein containing two or more polypeptide chains (subunits); determined by the number, relative positions, and interactions of the subunits.

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20
Q

van der Waals interactions

A

A weak electrical attraction between two hydrophobic side chains. Often contributes to tertiary structure in proteins.

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21
Q

oligopeptide

A

A chain composed of fewer than 50 amino acids linked together by peptide bonds. Often referred to simply as peptide.

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22
Q

cellulose

A

A structural polysaccharide composed of b-glucose monomers joined by b-1,4-glycosidic linkages. Found in the cell wall of algae, plants, bacteria, fungi, and some other groups.

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23
Q

chitin

A

A structural polysaccharide composed of N-acetylglucosamine monomers joined end to end by b-1,4-glycosidic linkages. Found in cell walls of fungi and many algae, and in external skeletons of insects and crustaceans.

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24
Q

phosphorylase

A

An enzyme that breaks down glycogen by catalyzing hydrolysis of the a-glycosidic linkages between the glucose residues.

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25
Q

peptidoglycan

A

A complex structural polysaccharide found in bacterial cell walls.

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26
Q

Simple sugars differ in what aspects?

A

1) The location of the carboxyl group
2) The number of carbon atoms present
3) The spatial arrangement of the atoms especially the hydroxyl groups

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27
Q

amylase

A

Any enzyme that can break down starch by catalyzing hydrolysis of the glycosidic linkages between the glucose residues.

28
Q

glycoprotein

A

Any protein with one or more covalently bonded carbohydrate groups. Used by cells as identification

29
Q

C-O vs. C-C C-H bonds

A

C-C and C-H bonds have more free energy because electrons are shared by atoms with low electronegativity

30
Q

glycerol

A

A three-carbon molecule that forms the “backbone” of phospholipids and most fats.

31
Q

ester linkage

A

The covalent bond formed by a condensation reaction between a carboxyl group (–COOH) and a hydroxyl group (–OH). Ester linkages join fatty acids to glycerol to form a fat or phospholipid.

32
Q

amphipathic

A

Containing hydrophilic and hydrophobic elements.

33
Q

If a micelle is formed the fatty acid tails would face in what direction?

A

inward

34
Q

What are the type of elements that are the most permeable in a lipid bilayer to the least permeable?

A

Small nonpolar(O2 CO2), small uncharged polar(H2O), large uncharged polar(glucose) and ions(Na, Cl)

35
Q

saturated fat

A

Referring to fats and fatty acids in which all the carbon-carbon bonds are single bonds. Such fats have relatively high melting points

36
Q

unsaturated fat

A

Referring to fats and fatty acids in which at least one carbon-carbon bond is a double bond. Double bonds produce kinks in the fatty acid chains and decrease the compound’s melting point

37
Q

Function of cholesterol in a membrane?

A

Decreases cell membrane permeability and stabilizes membrane

38
Q

hypertonic

A

Comparative term designating a solution that has a lower solute concentration, and therefore a higher water concentration, than another solution.

39
Q

hypotonic

A

Comparative term designating a solution that has a greater solute concentration, and therefore a lower water concentration, than another solution

40
Q

fluid mosaic model

A

The widely accepted hypothesis that the plasma membrane and organelle membranes consist of proteins embedded in a fluid phospholipid bilayer.

41
Q

What are the three forms of transport proteins

A

Channels, transporters and pumps

42
Q

Sodium Potassium Pump

A

A transmembrane protein that uses the energy of ATP to move three sodium ions out of the cell and two potassium ions in. Also called Na+/K+-ATPase.

43
Q

endothermic

A

Referring to a chemical reaction that absorbs heat.

44
Q

exothermic

A

Referring to a chemical reaction that releases heat.

45
Q

first law of thermodynamics

A

The principle of physics that energy is conserved in any process. Energy can be transferred and converted into different forms, but it cannot be created or destroyed.

46
Q

entropy

A

A quantitative measure of the amount of disorder of any system, such as a group of molecules.

47
Q

second law of thermodynamics

A

The principle of physics that the entropy of the universe or any closed system increases during any spontaneous process.

48
Q

What two factors determine spontaneous reactions?

A

1) products have lower potential energy than reactants.

2) Products are less ordered than reactants

49
Q

Gibbs free energy change

A

measure of the change in potential energy and entropy that occurs in a given chemical reaction. Calculated as DG = DH – T DS, where DH is the change in potential energy, T is the temperature in kelvins, and DS is the change in entropy. DG < 0 for spontaneous reactions and >0 for nonspontaneous reactions.

50
Q

exergonic

A

Referring to a chemical reaction that can occur spontaneously, releasing heat and/or increasing entropy, and for which the Gibbs free-energy change (DG) < 0

51
Q

endergonic

A

Referring to a chemical reaction that can occur spontaneously, releasing heat and/or increasing entropy, and for which the Gibbs free-energy change (DG) < 0

52
Q

Why are some exothermic reactions nonspontaneous?

A

Because they have a high potential energy and release heat so DG remains above 0.

53
Q

Why do some reactions only become spontaneous at higher temperatures?

A

Acording to Gibbs free energy change DG = DH - TDS. Meaning that at higher temperature DG has the possibilty of becoming negative which means a spontaneous reaction.

54
Q

activation energy

A

The amount of energy required to initiate a chemical reaction; specifically, the energy required to reach the transition state.

55
Q

transition state

A

A high-energy intermediate state of the reactants during a chemical reaction that must be achieved for the reaction to proceed

56
Q

The stabilization of the transition state is caused by what part of the enzyme?

A

R-groups

57
Q

cofactor

A

A metal ion or small organic compound that is required for an enzyme to function normally. May be bound tightly to an enzyme or associate with it transiently during catalysis.

58
Q

coenzyme

A

A small organic molecule that is a required cofactor for an enzyme-catalyzed reaction. Often donates or receives electrons or functional groups during the reaction.

59
Q

allosteric regulation

A

Regulation of a protein’s function by binding of a regulatory molecule, usually to a specific site distinct from the active site, causing a change in the protein’s shape.

60
Q

competitive inhibition

A

Inhibition of an enzyme’s ability to catalyze a chemical reaction via a nonreactant molecule that competes with the substrate(s) for access to the active site.

61
Q

“Saturation Kinetics” of enzymes

A

Enzymes reach a certain point where they cannot accept substrates any faster no matter the concentration

62
Q

substrate

A

(1) A reactant that interacts with an enzyme in a chemical reaction. (2) A surface on which a cell or organism sits.

63
Q

What variables affect enzyme efficiency?

A

Substrate concentration, enzyme-substrate relation, temperature and ph

64
Q

phosphorylation

A

The addition of a phosphate group to a molecule.

65
Q

cellular respiration

A

A common pathway for production of ATP, involving transfer of electrons from compounds with high potential energy(often NADH and FADH2) to an electron transport chain and ultimately to an electron acceptor(often oxygen)

66
Q

glycolysis

A

A series of 10 chemical reactions that oxidize glucose to produce pyruvate and ATP. Used by all organisms as part of fermentation or cellular respiration.

67
Q

What are the steps of cellular respiration?

A

1) Glycolysis
2) Pyruvate Processing
3) Citric acid cycle
4) Electron transport and chemiosmosis

Biology (15 decks)

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