Exam 1 - Last Minute Concepts Flashcards

1
Q

Polypeptides

A

A series of amino acids

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2
Q

Proteins

A

A series of polypeptides

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3
Q

Genetic Code Characteristics

A

Universal, unambiguous, non-overlapping, commaless

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4
Q

DNA Structure

A

Double helix, composed of nucleotides containing the four bases

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5
Q

Purines

A

Adenine, Guanine

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6
Q

Pyrimidines

A

Cytosine, Thymine

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7
Q

Watson and Crick

A

DNA is a double stranded helix with antiparallel strands and bases linked with hydrogen bonding

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8
Q

Phosphodiester Bond

A

5 carbon, 5 carbon bond between 2 sugars

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9
Q

Replication

A

DNA to DNA in the nucleus

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10
Q

Transcription

A

DNA to mRNA in the nucleus

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11
Q

Translation

A

RNA to protein in the ribosome

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12
Q

Meselson and Stahl

A

Replication of DNA to be semiconservative, meaning a parent strand is the template for synthesis of a new strand. DNA helixes contain one parent stand and one newly synthesized strand each

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13
Q

Helicase

A

Unwinds the stand for replication

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14
Q

RNA Primase

A

Sets up for RNA primer

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15
Q

DNA Polymerase II

A

Elongates both the leading and lagging strand in DNA replication

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16
Q

DNA Polymerase I

A

Removes the old RNA and replaces it with DNA

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17
Q

DNA Ligase

A

Catalyzes the formation of the phosphodiester bond linking the Okazaki fragments

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18
Q

RNA Polymerase II

A

Elongates in transcription

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19
Q

RNA Characteristics

A

Single stranded, the sugar molecule is a ribose not a deoxyribose, the fourth base in uracil not thymine

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20
Q

Messenger RNA

A

Message or direction on how to make a protein

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21
Q

Transfer RNA

A

Matches up amino acids with the RNA message

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22
Q

Ribosomal RNA

A

Used to bind the message

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23
Q

Four Binding Sites

A

Transfer, Amino acids, Polypeptide, Exit

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24
Q

Transer site

A

tRNA first lands here

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25
Q

Amino acid site

A

tRNA anticodon binds to mRNA codon

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26
Q

Polypeptide Site

A

tRNA adds its amino acid to the growing polypeptide chain

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27
Q

Exit Site

A

Where tRNA resides without its amino acid before leaving the ribosome and going back to the cytosol to pick up another amino acid

28
Q

Bond strength depends on

A

Temperature, pressure, bond angle, environment

29
Q

What shape does water make

A

Tetrahedron

30
Q

Covalant Bond

A

Sharing of pairs of electrons between atoms or between atoms and other covalent bonds

31
Q

Oxygen is an electron _____

A

Hog

32
Q

Water is a __________ ____________ bond

A

Polar covalent

33
Q

Polarity

A

An uneven distribution of electron density within a molecule

34
Q

We are always moving to _____________ but…?

A

Equilibrium, but not every equilibrium is a good one

35
Q

Hormone that plays a role in diabetes insipidus

A

ADH

36
Q

Keq > 1

A

Favours the product

37
Q

Keq < 1

A

Favours the reactant

38
Q

Le Chatelier’s Principle

A

If a chemical system in equilibrium is disturbed, the system will adjust to restore equilibrium

39
Q

Buffer

A

Resist changes in pH upon the addition of small amounts of either acid or base

40
Q

Human Blood pH levels

A

7.35-7.45

41
Q

Acidosis

A

pH lower than 7.35

42
Q

Alkalosis

A

pH above 7.45

43
Q

Three homeostasic regulators of hydrogen ions

A

Chemical, respiratory, renal

44
Q

Chemical Buffer system

A

First to respond, tie up excess acids and bases temporarily

45
Q

Respiratory System

A

Second to respond, removes CO2 from the body (carbonic acid)

46
Q

Renal Buffer System

A

Third to respond, most potent, kidneys removed metabolic acids

47
Q

Holoenzyme

A

Active enzyme with its nonprotein component

48
Q

Apoenzyme

A

Inactive enzyme without its non-protein moiety

49
Q

Cofactor

A

Nonprotein moiety is a metal ion

50
Q

Coenzyme

A

Small organic molecule moiety

51
Q

Michealis Menten Equation

A

S - concentration of the substrate

52
Q

Low Km

A

High affinity because a low substrate concentration is needed to saturate the enzyme (tight binding)

53
Q

High Km

A

Low affinity because a high substrate concentration is needed to saturate the enzyme (weak binding)

54
Q

Inhibitor

A

Any substance than can diminish the velocity of an enzyme catalyzed reaction

55
Q

Irreversible Inhibitor

A

Bind to enzymes through covalent bonds

56
Q

Reversible Inhibitors

A

Bind to enzymes through non-covalant bonds

57
Q

Competitive Inhibition

A

Binds reversibly to the same site as the substrate. Increases kM

58
Q

Noncompetitive Inhibition (ALLOSTERIC)

A

Inhibitor and substrate bind to different sites on the enzyme with a covalent bond. Decrease vmax because adding more substrate won’t help

59
Q

Positive Allosteric

A

Activates

60
Q

Negative Allosteric

A

Inhibits

61
Q

Homotrophic

A

Substrate of that enzyme

62
Q

Heterotrophic

A

Substrate of anything else

63
Q

Delta G < 0

A

The reaction is spontaneous

64
Q

Delta G = 0

A

The reaction is at equilibrium

65
Q

Delta G > 0

A

The reaction is non-spontaneous