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General Biology I > Chapter 3: Lipids, Carbohydrates, and Nucleic Acids > Flashcards

Chapter 3: Lipids, Carbohydrates, and Nucleic Acids Flashcards

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1
Q

Polymers from via _________________(1). Polymers break via _________________(2)

A

(1) Condensation
(2) Hydrolysis

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2
Q

What is dehydration/condensation?

A

The removal of water to from a covalent bond between monomers

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3
Q

What is hydrolysis?

A

The addition of water to break a covalent bond between monomers in a polymer

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4
Q

What are macromolecules? How do they form?

A

Large molecules prevalent in all organisms

Includes Lipids, carbohydrates, nucleic acids, proteins

Formed by endergonic condensation reactions that form covalent bonds between smaller molecules

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5
Q

Is the formation of macromolecules exergonic or endergonic?

A

Endergonic

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6
Q

Draw a hydroxyl functional group.

A

refer to notes

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7
Q

Draw a phosphate functional group.

A

refer to notes

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8
Q

Draw a carboxyl functional group.

A

refer to notes

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9
Q

Draw a amino functional group.

A

refer to notes

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10
Q

What are lipids defined by? What are some example of lipids?

A

Their insolubility in water

Ex. fats, oils

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11
Q

Are lipids hydrophobic or hydrophilic? Why?

A

Lipids are hydrophobic because of their many non polar covalent bonds

Contain mostly C—C and C—-H npon polar bonds, which have high schemical-bond energy.

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12
Q

What is the melting temperature of lipids determined by?

A

The size and how closely the molecules pack together(van der Waals interactions hold them together

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13
Q

What is a triglyceride?

A

Fats and oils, made of three fatty acids and one glycerol

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14
Q

What is a fatty acid?

A

a fatty acid is a carboxylic acid with a carboxylic acid consisting of a hydrocarbon chain and a terminal carboxyl group, which is either saturated or unsaturated.

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15
Q

What is glycerol?

A

A 3 carbon compound

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16
Q

What is a saturated fatty acid? What is the state at room temp?

A

All bonds between carbon atoms are single; they are saturated with hydorogens; pack together tightly; solid at room temp

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17
Q

What is an unsaturated fatty acid?

A

One or more double bonds between carbons; causes kinks in the chain and prevent molecules from packing together tightly; liquid at room temp

ex. coconut oil

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18
Q

How to compare the melting points of unsaturated vs saturated?

A

The more saturated something is, the higher its melting point

If something is 50% saturated and 50% unsaturated, it will be a solid

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19
Q

What is a lipoprotein? What is its purpose?

A

With certain proteins, phospholipids can form single-layer spheres with hydrophobic interiors and hydrophilic exteriors.

Lipoproteins are used for transporting lipids in aqueous solutions, such as triglycerides and cholesterol in the blood.

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20
Q

Is cholesterol a lipid?

A

Yes, it is a type of fat

It helps with fluidity and strength

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21
Q

What are some lipid functions?

A

Membranes, cholesterol, hormones(ex. sex hormones like estrogen and testosterone)

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22
Q

Is a phospholipid hydrophobic or hydrophilic?

A

It has a hydrophilic head and a hydrophobic tail

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23
Q

What are carbohydrates?

A

Linked carbons bonded to functional groups containing O and H, such as hydroxyl

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24
Q

What are lipids? What are the monomers of lipids?

A

Fats are a class of lipids containing two kinds of monomers, fatty acids, and glycerol.

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25
Q

Fatty acids are amphipathic. What does this mean?

A

a chemical compound containing both polar (water-soluble) and nonpolar (not water-soluble) portions in its structure.

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26
Q

Is a triglyceride hydrophobic or hydrophilic?

A

Hydrophobic

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27
Q

Are phospholipids amphipathic?

A

yes

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28
Q

Draw a phospholipid

A

refer to notes

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29
Q

What are simple sugars?

A

Carbohydrates with 12 or fewer carbons

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30
Q

What are monosaccharides?

A

Five or six carbons, usually in a ring(pentoses and hexoseS)

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31
Q

What is a disaccharide? What bond are they connected by?

A

Two monosaccharides linked by a glycosidic bond.

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32
Q

Mono and disaccharides can be ____________________(1) to proteins or lipids, modifying their ____________________(2)

A

(1) covalently bonded
(2) solubility and function

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33
Q

What is the format for naming glycosidic bonds?

A

(alpha/beta) (numbers) (glycosydic/peptidyl) bond

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34
Q

How to know if something is alpha or beta?

A

if the oxygen’s flip flop in position –> beta

if the oxygens don’t flip flop –> alpha

35
Q

What is an oligosaccharide? What bond are they connected by?

A

Three to 10 monosaccharides joined by glycosidic bonds

36
Q

oligosaccharides sometimes bind to proteins and lipids on cell membranes. What is the function of this?

A

they function as recognition signals

37
Q

What are polysaccharides?

A

Polymers of hundreds to thousands of monosaccharides

38
Q

Know how to number carbons in a sugar

A

the carbon hanging in the breeze has the highest numerb

39
Q

What are linear chains of polysaccharides?

A

Monomers attached via 1,4 glycosidic bonds; branched chains are attached via 1,6 glycosidic bonds

40
Q

Give examples of linear polysaccharide chains. Give examples of branched polysaccharides.

A

Linear: cellulose and chitin

\branched: starches, glycogen

41
Q

What are nucleic acids?

A

Polymers that store, transmit, and express hereditary(genetic) infromation

includes DNA(deoxyribonucleic acid) and RNA(ribonucleic acid)

42
Q

What are the monomers of nucleic acids?

A

Nucleotides, which contain a pentose sugar + N-containing base + phosphate grup

43
Q

What is a nucleoside?

A

Pentose sugar + N-containing base

44
Q

What pentose sugars do DNA and RNA conaitna?

A

DNA: deoxyribose(has just the H

RNA: ribose(had the OH, which is very reactive)

45
Q

What is a pyrimidine and purine?

A

Pyrimidine: single ring

purine: double rings

46
Q

Which bases are pyrimidines?

A

C, U, T, P

(cutie py)

47
Q

Which bases are purines?

A

A G

Pure as gold

48
Q

Nucleic acids grow in the _________________(1) direction.

A

(1) 5’ to 3’

49
Q

Nucleotides bond in _________________(1) to form __________________(2) bonds.

A

(1) condensation reactions
(2) phosphodiester bonds

50
Q

What are oligonucleotides?

A

Have up to 20 monomers, mostly RNA moleucles

51
Q

What are polynucleotides?

A

composed of several nucleotide monomers with covalent bonds in a chain.

52
Q

RNA is ______________(1) and DNA is __________________(2). IN DNA, the two strands come together by __________________________(3).

A

(1) single stranded
(2) double stranded
(3) complementary base apriing

53
Q

What are the complementary base pairs?

A

A and T(or U)

G and C

54
Q

The two DNA strands run _______________(1), which means they run in opposite directions. The funds of the ladder are formed by _______________(2) and the sides of the ladder are formed by _______________(3)

A

(1) antiparallel
(2) hydrogen-bonded bases
(3) sugar-phosphate groups

55
Q

The bonds holding the two strands of DNA together are _______________(1). Base pairs can be separated with only a _______________(2)

A

(1) hydrogen bonds
(2) small amount of energy

56
Q

RNA is usually single stranded but often ______________________________(1). The double strand regions give the molecule a 3-D shape that affects how it interacts with other molecules.

A

(1) folds back on itself to form short double-strand region

57
Q

What is transcription?

A

Information encoded in DNA base sequences is used to synthesize RNA

58
Q

What is translation

A

Information in RNA base sequences is used to synthesize proteins

59
Q

What are genes?

A

DNA sequences that encode specific proteins and are trasncribed into RNA

60
Q

What is the genome?

A

Complete set of DNA in a. living organism

61
Q

List the four macromolecules int eh quantity in which they appear most in the body.

A

proteins>nucleic acids>carbs>lipids

62
Q

What is cystic fibrosis caused by?

A

problems with one protein

63
Q

What are the monomers of proteins?

A

Amino acids

64
Q

What is the structure of amino acids?

A

A central carbon atom(the alpha carbon) connected to an amino group(NH2 or NH), a carboxyl group(COO-), a hydrogen atom, and a side-chain(R group)

65
Q

Amino acids are linked together by ___________________(1) to form a protein.

A

(1) peptide bonds

66
Q

The amino terminus is known as the _______________(1). The carboxyl terminus is known as the _______________(2). New amino acids are always added to the _______________(3) of a growing chain.

A

(1) N- terminus
(2) C-terminus
(3) c-terminus

67
Q

What are the four categories of amino acids?

A
  1. Polar and charged
  2. Polar and uncharged
  3. Nonpolar(S-CH3 is non polar)
  4. special cases
68
Q

What are the three special cases that should be memorized?

A

Cysteine(CH2 - SH)

Glycine(just an H)

Proline(3(CH2))

69
Q

A chain of interconnected amino acids will not remain linear in aqueous solution; it will __________(1) into an energetically more stable structure.

A

(1) fold

The folded structure seeks to minimize exposure of non polar amino cid side chains to surrounding water while maximizing exposure of polar and charged groups. Non polar side chains are largely hidden in the interior of a folded chain.

70
Q

The folded structure of a protein that is biologically active is called _______________(1).

A

(1) the native structure

71
Q

What is protein denaturation?

A

Denaturations refers to the disruption of the folded structure of a protein. Heat, chemicals, pH changes, etc. can disrupt weaker bonding interactions in a bonding.

72
Q

Give some examples of diseases that are caused by misfolded or aggregated proteins.

A
  • ALzheimer’s, cystic fibrosis, Gaucher’s disease, Huntington’s disease, Parkinson’s disease, sickle cell anemia
73
Q

What constitutes a protein backbone?

A

All of the amino acids linked together but not counting their side chains(R groups)

74
Q

What is a polypeptide chain?

A

One string of amino acids

75
Q

What is a protein?

A

Composed of one or more polypeptide chains

76
Q

What is the primary structure of a protein?

A

The sequence of amino acids in a single polypeptide chain

Have covalent peptide bonds that link amino acids

77
Q

What is secondary structure?

A

Regular, repeated spatial patterns of local regions of a polypeptide chain, folded by hydrogen bonding.

Can have beta pleated sheets or alpha helixes

Hydrogen bonds indicated with dotted or dashed line

78
Q

What is the tertiary structure?

A

Entire polypeptide chain is bent and folded upon itself; results in the definitive 3d shape

beta pleats and alpha helixes connected by COVALENT disulphide bridges

have disulfite bridge(only covalent bonds), ionic bonds, hydrogen bonding, hydrophobic interactions between r groups

79
Q

What is quaternary structure?

A

Two or more polypeptide chains(subunits) come together to forma. larger structure. Typically stabilized by non-covalent interactions, but can also occur through disulphide bonds.

have disulfite bridge(only covalent bonds), ionic bonds, hydrogen bonding, hydrophobic interactions between r groups

80
Q

What are catalysts?

A

Substances that speed up reactions without being permanently altered(don’t get used up)

81
Q

Enzymes are biological catalysts. How do they work?

A

Enzymes temporarily bind to their substrates(reactants) to catalyze a chemical reaction. Substrates bind in the enzymes active site. they lower the activation energy needed to reach transition state

82
Q

What is a noncompetitive inhibitor?

A

A noncompetitive inhibitor binds at a site distinct from the active site, affecting enzyme shape and function. it prevents substrate binding or slows the reaction rate

83
Q

The site where the inhibitor binds is called the _______________(1)

A

(1) allosteric site

84
Q
A

General Biology I (14 decks)

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