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Bio 1 > Exam 1 > Flashcards

Exam 1 Flashcards

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Biology 101 flashcards
1
Q

Weak interactions between non polar molecules that are close

A

Van der waals forces

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2
Q

Accepts H+

A

Bases

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3
Q

Donates H+

A

Acid

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4
Q

Acts as both acid and base

A

Water

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5
Q

Mix of weak acid and it’s conjugate base (vice versa)

A

Buffer

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6
Q

Measure of H+

A

pH

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7
Q

pH formula

A

-log[H+]

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8
Q

Hydrochloric Acid (HCl)

A

Strong Acid; fully dissociates to make H+ and Cl- in water

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9
Q

Carbonic Acid (H2CO3)

A

Weak Acid; partially dissociates in water to form H+ and HCO3-

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10
Q

Nitric Acid

A

Strong Acid; fully dissociates to make H+ and NO3-

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11
Q

Acetic Acid

A

Weak Acid; partially dissociates to make H+ and CH3COO-

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12
Q

Phosphoric Acid (H3PO4)

A

Weak acid; partially dissociates into H+ ions and H2PO4-, HPO4(2-), and PO4(3-)

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13
Q

Sulfuric Acid (H2SO4)

A

Strong Acid; Fully dissociates to form HSO4- and H+

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14
Q

Ammonia (NH3)

A

Weak base; partially dissociates in water to form NH4+ and OH-

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15
Q

Sodium Hydroxide (NaOH)

A

Strong base; fully dissociates to form Na+ and OH-

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16
Q

Potassium Hydroxide (KOH)

A

Strong base; fully dissociates to form K+ and OH-

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17
Q

Methyl Amine (CH3NH2)

A

Weak base; partially dissociates in water to form CH3NH3+ and OH-

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18
Q

Sodium Hypochlorite (NaOCL)

A

Weak base

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19
Q

Functional Group

A

Determines how molecules interact with others

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20
Q

Carbohydrates

A

Variably sized sugar molecules usually with formula (C1H2O1)n. Characterized by number of sugars.

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21
Q

Carbohydrate functions include

A

Storing energy
Transporting stored energy
Be arranged to form other molecules
Form extra cellular support structures

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22
Q

Monosaccharides

A

Simple sugars; monomer of complex carbs; used as energy source; exists as ring or chain

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23
Q

Disaccharides

A

Two simple sugars linked by covalent bonds

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24
Q

Oligosaccharides

A

Formed by several monosaccharides; often covalently bonded to proteins and lipids on cell surfaces where they serve as recognition signals

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25
Q

Polysaccharides

A

Larger polymers of monosaccharides; some are branched

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26
Q

Glycosidic Bonds

A

Bonds by which di, oligo, and polysaccharides are held together

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27
Q

Condensation Reaction

A

Results in formation of covalent bonds between monomers; forms polymers and creates water; new covalent bond between monomers and water is created

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28
Q

Hydrolysis Reaction

A

Breaks down polymers into monomers and consume water

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29
Q

Lipids

A

Nonpolar hydrocarbons that have various roles in cells; defined by insolubility in water

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30
Q

Fats and Oils

A

Type of lipid; triglycerides that store energy

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31
Q

Triglyceride

A

3 fatty acids and 1 glycerol connected with an ester linkage (formed through condensation reaction)

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32
Q

Fats are

A

Solid at room temp

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33
Q

Oils are

A

Liquid at room temp

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34
Q

Phospholipid

A

Type of lipid; 2 fatty acids bound to glycerol with a phosphate; amphipathic: head is hydrophilic phosphate group and tail is hydrophobic fatty acid chains

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35
Q

Carotenoids

A

type of lipid; light absorbing pigments

36
Q

Steroids

A

Multiple rings that share carbon atoms; cholesterol, messenger molecules, hormones, etc

37
Q

Wax

A

Long chain alcohol bound ton an unsaturated fatty acid

38
Q

Nucleic Acids

A

Informational macromolecules

39
Q

Monomer of nucleic acids

A

Nucleotides

40
Q

Polymer of nucleic acids

A

DNA and RNA

41
Q

DNA molecules vary in their

A

sequence of bases

42
Q

Chargaff’s Rule

A

[A]=[T], [C]=[G]= 50%

43
Q

Purines

A

Type of nitrogenous base; double ringed; adenine and guanine

44
Q

Pyrimidines

A

Type of nitrogenous base; single ringed; cytosine and thymine

45
Q

What kind of backbone do oligonucleotides have?

A

Sugar-phosphate backbone; always attaches to carbon #5

46
Q

Differences between RNA and DNA

A

RNA single-stranded vs DNA double
RNA has 2 OH groups, DNA has OH and H (RNA more reactive)
Sugar in RNA is ribose vs sugar in DNA is deoxyribose

47
Q

Nucleotide ATP

A

Adenine monomer of RNA; used as energy carrier

48
Q

Phosphodiester Bond

A

Links nucleotides in a strand of DNA (covalent bonds); between phosphate group at 5 carbon location and hydroxyl at 3 carbon location

49
Q

What did Rosalind Franklin’s Photo 51 reveal about DNA?

A

Double helix
Bases are on inside of each strand and sugar-phosphate groups are on inside
Diameter: 2nm
Number of nucleotides per turn=10
Chain is antiparallel

50
Q

Key features of DNA

A

Double Helix
Right-handed (turns to right)
Antiparallel (one strand has free 3’ hydroxyl group other strand has free 5’ phosphate group)
Strands are held together by hydrogen bonding between complementary bases
Outer edges of the bases are exposed in major and minor grooves (major=bigger)

51
Q

Monomers of Protein

A

Amino Acids

52
Q

Gene

A

A sequence of DNA that contains the info to make one protein

53
Q

One gene, one enzyme hypothesis

A

Each gene contains the info needed to make a single enzyme

54
Q

RNA polymerase

A

The enzyme that synthesizes RNA according to the information provided by the sequence of bases in a particular stretch of DNA; transcription

55
Q

Coding strand of DNA

A

Has same polarity and sequence as mRNA

56
Q

mRNA

A

Carries info from DNA to site of protein synthesis

57
Q

Template strand of DNA

A

Complementary to RNA

58
Q

What reads mRNA to produce protein?

A

Ribosomes

59
Q

Transcription

A

First process in gene expression; is the process by which hereditary info in DNA is copied to mRNA

60
Q

Translation

A

Second process in gene expression; process by which info in mRNA is used to synthesize proteins

61
Q

What determines the sequence of amino acids in a protein

A

The sequence of bases in the mRNA

62
Q

Genetic code

A

A triplet code, with a three base sequence called a codon specifying a single amino acid

63
Q

Four characteristics of the genetic code

A

Redundant; all amino acids except Met and TRP are coded for by more than one codon
Conservative; when several codons specify the same amino acid, the first two bases of the codons are almost always identical
Unambiguous; a single codon never codes for more than one amino acid
Universal; With few exceptions, all organisms have the same genetic code

64
Q

Start Codon

A

AUG

65
Q

Stop Codons

A

UAA, UAG, UGA

66
Q

What dictates protein’s functions

A

Folding of its polypeptide chains into specific shapes

67
Q

Primary Structure of protein

A

The sequence of the amino acids in a polypeptide chain

68
Q

Which of the two isomers of amino acids are found in physiological contexts?

A

L-alanine, not D-alanine

69
Q

What dictates amino acid’s properties

A

Amino acid side chains aka r-groups

70
Q

Which amino acids have polar, hydrophilic side chains that are uncharged?

A

Serine, Threonine, Asparagine, Glutamine, Tyrosine

71
Q

Which amino acids have charged hydrophilic side chains

A

Arginine, Histidine, Lysine, Aspartic Acid (-), Glutamic Acid (-)

72
Q

Which amino acids have hydrophobic side chains

A

Alanine, Isoleucine, Leucine, Methionine, Phenylalanine, Tryptophan, Valine

73
Q

Which amino acids don’t fit any categories

A

Cysteine, Glycine, Proline

74
Q

Amino groups in amino acids

A

Accept H+ (basic)

75
Q

Carboxyl groups in amino acids

A

Donates H+(acidic)

76
Q

Influences to protein folding include

A

H bonds
pH
temp
van dar waals forces
hydrophobic interactions

77
Q

Secondary structure of a protein

A

Determined and stabilized by hydrogen bonding with the backbone of amino acids (may form alpha helix or beta pleated sheets)

78
Q

Tertiary structure

A

How a protein folds in 3D because of interactions between R groups; stabilized by hydrogen bonds, disulfide bridges, hydrophobic interactions

79
Q

Quaternary Structure

A

Association of polypeptides with other polypeptides

80
Q

What happens if a chemical treatment were used to disrupt the secondary and tertiary structure of a protein

A

It would become denatured (unfolded) and it won’t function

81
Q

Urea

A

Highly polar molecule that disrupts hydrogen and ionic bonds

82
Q

B-mercaptoethanol

A

Can reduce/break disulfide bridges

83
Q

Proteins have very specific binding partners to which they bind

A

Non-covalently

84
Q

What is specificity in binding of protein partners determined by

A

Shape: should be general fit between protein and other molecule
Chemistry: surface R groups can interact with other molecule through non-covalent interactions

85
Q

Chaperone Proteins

A

Protects proteins from inappropriate binding and also helps new proteins with folding

Bio 1 (8 decks)

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