Biological Molecules Unit 1 Flashcards

1
Q

In a Eukaryotic Cell where would you find DNA & RNA? (6)

A

Nucleus, Cytosol, Mitochondrion, Chloroplast, Lysosome, Plant vacuole

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2
Q

What linked patterns make up large molecules?

A

Polymers, and Monomers

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3
Q

What causes polymers to form and break up?

A

Polymers form via dehydration reactions (loss of water molecule), and are broken up by hydrolysis reactions (gain water molecule)

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4
Q

What is the general formula for carbohydrates?

A

(CH2O)n

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5
Q

What is a monosaccharide, and how many carbon atoms does it have?

A

The most basic form of carbohydrate, and between 3-7 carbon atoms

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6
Q

What is a disaccharide and what links it together?

A

A disaccharide is two monosaccharides attached with a glycosidic linkage

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7
Q

How are glycosidic linkages formed?

A

Dehydration reaction

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8
Q

What is a glycosidic linkage?

A

A type of covalent bond that joins carbohydrate molecules to another group

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9
Q

What polysaccharides make up starch and what organisms utilise starch as their main storage?

A

Amylose and amylopectin (polymers of glucose), and plants and some algae

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10
Q

What is the main storage polysaccharide for animals, and what is it similar to?

A

Glycogen, and similar to amylopectin (glucose polymer in plants/algae)

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11
Q

What are the enzymes that hydrolyse starch and glycogen in animals?

A

Amylases

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12
Q

What is the principal structural polysaccharide in plant cell walls?

A

Cellulose

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13
Q

In plants, what are the enzymes that hydrolyse cellulose called?

A

Cellulases

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14
Q

What are the five(5) main functions of carbohydrates?

A

Storage of energy & materials, transport of energy and materials, energy generation, building material (especially in cells walls of plants/protists, and cell surface activities including recognition and signalling

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15
Q

What are lipids, and what are they made of, and are they water soluble?

A

Lipids are fats, mainly consisting of hydrocarbons (C-C, C-H bonds), they aren’t water soluble

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16
Q

What two parts make up fatty acids?

A

A hydrophilic (water loving) carboxyl group, and an unbranched hydrophobic (water fearing) hydrocarbon chain

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17
Q

What makes fatty acids amphipathic?

A

It’s b/c they have both a hydrophobic, and hydrophilic region

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18
Q

What are four(4) structural variations in fatty acids?

A

Length of carbon chain, saturated (no C-C double bonds) or unsaturated (1 or more C-C double bonds), location of the double bonds, and cis & trans configuration at double bonds and its almost alway cis (introduces bend)

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19
Q

What is a triacylglycerol?

A

They’re fatty acid esters of glycerol (3 carbon chain)

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20
Q

Triacylglycerol room temperature state in animals and plants?

A

Animals- solid at room temperature, make up most of common fat
Plants- liquid at room temperature (oil)

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21
Q

What are phospholipids, and describe their structure.

A

A type of lipid that spontaneously forms a bilayer once placed in a aqueous solution, and has a hydrophilic head, and two hydrophobic tails

22
Q

What are steroid and what is their function?

A

Steroid are lipids and produce hormones (estrogen & testosterone)

23
Q

What are the six(6) main functions of lipids?

A

Membrane structure, energy storage, energy generation, thermal insulation, signalling and buoyancy

24
Q

What are proteins?

A

Polymers composed of many amino acid monomers

25
Q

What are amino acids?

A

Small molecules that are the building blocks of proteins. Chemically it is a carboxylic acid and an amine group attached to a alpha carbon. See amino acid picture.

26
Q

How are amino acids attached together? And what do they form?

A

Amino acids are attached via a dehydration reaction, and form an unbranched polypeptide by forming peptide bonds w/ the amino acid residue

27
Q

What is a polypeptide, and what do they create?

A

Polypeptide is a polymer composed of many amino acid residues, and they form proteins.

28
Q

What are three(3) key features of a polypeptide?

A

A monotonous repeating N-C-C-N-C-C-N backbone, R groups extending from the backbone w/ differing orders from one polypeptide to another, and N-terminus (amino) and C-terminus (carboxyl) giving the polypeptide polarity.

29
Q

What are the four(4) levels of polypeptide structure?

A

Primary, secondary, tertiary, and quaternary

30
Q

How many tripeptides are possible?

A

20^3=8000, b/c there is 20 amino acid groups

31
Q

What are the four(4) main groups of biological molecules?

A

Lipids (fats & oils), Proteins (amino acids), Carbohydrates (sugars), and nucleic acids (DNA/RNA)

32
Q

What are the three(3) most common carbohydrates?

A

Glucose, fructose (plant sugar), and sucrose (glucose + fructose)

33
Q

What are the four(4) major examples of polysaccharides in organisms?

A

Starch, glycogen, cellulose, chitin

34
Q

What is the difference between alpha and beta glucose?

A

Positioning of 1 of the 4 hydroxyl groups. Alpha is when the -OH is below the carbon ring, and beta is when the -OH is above the carbon ring

35
Q

What is the primary structure of polypeptides/proteins?

A

The one-dimensional sequence of amino acid residues

36
Q

What is the secondary structure of polypeptides/proteins?

A

The three-dimensional shape resulting from the hydrogen bonding regions of the backbone that are close by in terms of the primary structure

37
Q

What two(2) shapes do the secondary structure polypeptides/proteins have?

A

Alpha helix, and beta pleated sheet

38
Q

What is the tertiary structure of the polypeptides/proteins?

A

The folded shape of the polypeptide arising from interactions among the R groups

39
Q

What is the quaternary structure of the polypeptides/proteins?

A

Assembly of two or more polypeptide chains into a functional complex, due again to interactions among the R groups.

40
Q

Do all functional proteins have quaternary structure?

A

No

41
Q

What are the nine(9) functions of proteins?

A

Catalysis of biochemical reactions by enzymes, Cytoskeleton & motility, Structural proteins, signalling molecules (insulin), transcription factors, cell surface receptors (chemical stimuli), defence (antibodies), storage (starch amino acids), Transport (hemoglobin movement)

42
Q

What are the two(2) types of nucleic acids, and describe them?

A

DNA-a double stranded helix held together mainly by complementary base pairing btwn strands
RNA-a single stranded, but can have some regions double helical structure resulting from intrastrand complementary base pairing

43
Q

What are the five(5) main components of DNA & RNA?

A

Base (rings containing C & N), sugar (ribose in RNA & deoxyribose in DNA), phosphate group (negative charge), nucleoside (base+sugar), nucleotide (base+sugar+phosphate groups)

44
Q

What are the four(4) main functions of nucleic acids?

A

Information storage (genes are made of DNA), information retrieval (gene expression), Energy currency (ATP,a ribonucleotide), and catalysis of some biochemical reaction by ribozymes)

45
Q

What are three(3) examples of modified types of molecules?

A

Glycoproteins, proteoglycans, and glycolipids

46
Q

Two(2) other molecules in cells that do not make up their own class?

A

Vitamins (small molecules), and secondary metabolites (molecules produced, but are not needed for basic universal processes

47
Q

How are nucleotides linked together?

A

By phosphodiester bonds to give a polynucleotide strand

48
Q

What is significant about the polynucleotide strand?

A

It has polarity, the 5’ & 3’ ends are different

49
Q

Describe the DNA double helix?

A

Consists of two polynucleotide strands held together firmly by complementary base pairings that run antiparallel to each other.

50
Q

What are the four(4) links named in DNA, and which pair together?

A

Adenine-Thymine, Cytosine-Guanine

51
Q

What groups does the main structure of proteins consist of? (4)

A

Central C (alpha carbon), amino group (NH2), carboxyl group (COOH), and a hydrogen atom

52
Q

What exactly happens when a protein becomes ‘denatured’?

A

Protein looses it’s higher order structure, but not its primary sequence. They’re usually non-functional