Biology Lecture 1: Molecular Biology; Cellular Respiration

Front 1

Water

Back 1

Universal solvent; 70-80% of a cell's mass; polar molecule with the ability to hydrogen bond

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Hydrolysis

Back 2

The breaking down of a compound by reacting with water

Front 3

Dehydration synthesis

Back 3

Builds up molecules by losing water molecules

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Lipid

Back 4

Biological molecule that has low solubility in water and high solubility in nonpolar organic solvents; hydrophobic

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Principal structural components of living cells

Back 5

Lipids, proteins, and carbohydrates

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Six major groups of lipids

Back 6

Fatty acids, triacylglycerols, phospholipids, glycolipids, steroids, terpenes

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Fatty acid

Back 7

Long chains of carbons ending in a carboxyl group; usually even in number;max number of carbons in humans is 24

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Saturated fatty acids

Back 8

Contain only C-C single bonds

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Unsaturated fatty acids

Back 9

Contain one or more C=C double bonds

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Triacylglycerols/Trigylcerides

Back 10

Three carbon backbone (gylcerol) attached to three fatty acids; store metabolic energy and provide thermal insulation and padding

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Adipocytes

Back 11

Specialized fat cells who cytoplasm contain almost nothing but trigylcerides

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Phospholipids

Back 12

Three carbon backbone (gylcerol) attached to two fatty acids (nonpolar) and one polar phosphate group; major component of most membranes

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Amphipathic

Back 13

A molecule that has a polar end that is attracted to water and a nonpolar end that is repelled by it

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Steroids

Back 14

17-carbon 4-ring system that contain hormones and are precursors to certain vitamins; regulate metabolic activities

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Proteins/Polypeptides

Back 15

Amino acids joined by peptide bonds

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Side chain

Back 16

A branched chain of amino acids attached to the alpha-carbon; often designated as the R group

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Primary structure

Back 17

The basic sequence of amino acids in a polypeptide or protein

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Secondary structure

Back 18

The arrangement of a polypeptide into a regular alpha helix, beta structure, or random coil configuration by the formation of intramolecular hydrogen bonds along the length of the chain; contribute to the confirmation of the protein

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Tertiary structure

Back 19

Three-dimension shape formed when polypeptides curl and fold

Front 20

Disulfide bond

Back 20

The covalent bond between sulfur atoms that binds two peptide chains or different parts of one peptide chain and is a structural determinant in many protein molecules

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Quaternary structure

Back 21

When two or more polypeptide chains form together

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Denature

Back 22

A change in the structure or protein which alters solubility and coagulation

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Two types of proteins

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Globular and Structural

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Globular proteins

Back 24

Function as enzymes, hormones, membrane pump and channels, membrane receptors, cellular transport and storage, etc.

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Structural proteins

Back 25

Maintain and add strength to the cellular and matrix structure.

Example: Collagen, the most abundant protein in the body

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Carbohydrates/Sugars/Saccharides

Back 26

Organic compounds that contain only carbon, hydrogen, and oxygen in a 1:2:1 ratio

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Glucose

Back 27

Most commonly occurring six-carbon carbohydrate; accounts for 80% of the carbs absorbed by humans

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Anomer

Back 28

A cyclic stereoisomer, such as a sugar, whose sole conformational difference involves the arrangement of atoms or groups in the aldehyde or ketone group

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Glycogen

Back 29

A polysaccharide that is the main form of carbohydrate storage in animals and occurs mainly in liver and muscle tissue; it is readily converted to glucose

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Starch

Back 30

A carbohydrate that is the chief form of stored energy in plants, especially wheat, corn, rice, and potatoes.

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Cellulose

Back 31

A complex carbohydrate that is composed of glucose; forms the main part of the cell wall in most plants

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Nucleotides

Back 32

Basic structural units of RNA and DNA composed of a five carbon sugar, a nitrogenous base, and a phosphate group; 5' - 3'

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Nitrogenous bases

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(most common) Adenine, Guanine, Cytosine, Thymine, and Uracil

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DNA

Back 34

Two polynucleotide chains in the form of a double helix, containing phosphate and the sugar deoxyribose linked by hydrogen bonds between the complementary bases A-T or C-G; Self-replicating, plays a central role in protein synthesis

Front 35

RNA

Back 35

A polymeric constituent of all living cells and many viruses, consisting of a long, usually single-stranded chain of alternating phosphate and ribose units with the bases adenine, guanine, cytosine, and uracil bonded to the ribose.

Front 36

ATP (adenosine triphosphate)

Back 36

Nucleotide that releases energy by hydrolysis into ADP during cell metabolism

Front 37

cAMP (cyclic Adenosine MonoPhosphate)

Back 37

Formed from ATP acts in the cell to regulate metabolic processes

Front 38

NAD (nicotinamide adenine dinucleotide)

Back 38

A coenzyme that occurs in many living cells and functions as an oxidizing or reducing agent in metabolic reactions.

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Minerals

Back 39

A solid homogeneous crystalline chemical element or compound that results from the inorganic processes of nature

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Enzymes

Back 40

Govern virtually all biological reactions; act as catalyst, lowering activation energy and increasing the rate of the reaction

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Substrate

Back 41

The base on which an organism lives; the substance upon which an enzyme acts

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Active site

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The position on the enzyme where the substrate binds

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Enzyme specificity

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Enzymes are designed to work only on specific substrates or a group of closely related substrates
(e.g. the lock-and-key-theory)

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Saturation kinetics

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As the relative concentration of a substrate increases, the rate of the reaction also increases but to a lesser degree until the max rate is achieved

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Coenzyme

Back 45

A non-protein organic substance that usually contains a vitamin or mineral and combines with a specific protein (apoenzyme) to form an active enzyme system

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Irreversible (enzyme) inhibitors

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Agents which bond covalently to enzymes and disrupt their function

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Competitive (enzyme) inhibitors

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Compete with substrates by binding reversibly with noncovalent bonds to the active site which blocks the substrate from binding.

Front 48

Noncompetitive (enzyme) inhibitors

Back 48

Bind noncovalently to an enzyme somewhere other than the active site and change the confirmation of the enzyme

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Zymogen/ Proenzyme

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Any of a group of proteins that are converted to active enzymes by partial breakdown, as by the action of an acid or other enzyme

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Allosteric regulation

Back 50

Modification of the enzyme configuration resulting from the binding of an activator or inhibitor at a specific binding site on the enzyme

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Metabolism

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Physical and chemical processes in an organism by which its material substance is produced, maintained, and destroyed, and by which energy is made available

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Anaerobic respiration

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Respiration in which oxygen is not required; fermentation, oxidizes NADH to NAD

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Aerobic respiration

Back 53

Respiration in which oxygen is required; produces about 36 net ATPs

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Glycolysis

Back 54

The first stage of anaerobic respiration where glucose is broken down into pyruvate

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Cytosol

Back 55

Fluid portion of living cells

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Substrate level phosphorylation

Back 56

Formation of ATP from ADP and inorganic phosphate using the energy released from the decay of high energy phosphorylated compounds as opposed to energy diffusion

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Mitochondria

Back 57

Functions as energy production in the cytoplasm of cells

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Acetyl CoA (acetyl coenzyme A)

Back 58

Transfers two carbons from pyruvate to the 4-carbon oxaloacetic acid to begins the Krebs cycle (citric acid cycle)

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Substrate-level phosphorylation

Back 59

Process of ATP production in the Krebs cycle

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Krebs cycle

Back 60

Aerobic metabolism of carbohydrates, proteins, and fatty acids, where carbon dioxide is produced, oxygen is reduced, and ATP is formed

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Electron transport chain (ETC)

Back 61

A set of proteins in the inner membrane of the mitochondrion that transfer hydrogen ions across a membrane

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ATP synthase/ oxidative phosphorylation

Back 62

An enzyme that allows protons to move through the mitochondrial membrane and trigger phosphorylation of ADP to ATP

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1 NADH

Back 63

Produces 2-3 ATPs

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1 FADH2

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Produces about 2 ATPs

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1 Glucose

Back 65

Produces 2 turns in the Krebs cycle

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Each turn in the Krebs cycle produces

Back 66

1 ATP, 3 NADH, and 1 FADH2

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Products and Reactants for Respiration

Back 67

Glucose + Oxygen → Carbon dioxide + Water