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DAT Prep > Molecules and Fundamentals of Biology > Flashcards

Molecules and Fundamentals of Biology Flashcards

Chapter one

1
Q

What are Ribose, Fructose and Glucose?

A

Monosaccharides

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2
Q

Ribose has how many carbons?

A

Five Carbons

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3
Q

Fructose has how many carbons?

A

Six Carbons

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4
Q

Glucose has how many carbons?

A

Six Carbons

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5
Q

What is a hydrolysis reaction?

A

Bond Broken by addition of water

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6
Q

What is Sucrose?

A

Glucose + Fructose disaccharide

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7
Q

What is Lactose?

A

Galactose + Glucose disaccharide

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8
Q

What is Maltose?

A

Glucose + Glucose disaccharide

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9
Q

What is Starch?

A

Energy storage for plants (alpha bonded)

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10
Q

What are the two types of starch?

A

Linear and Branched

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11
Q

What does linear starch consist of?

A

Amylose

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12
Q

What does branched starch consist of?

A

Amylopectin

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13
Q

What is glycogen?

A

Energy storage for humans (alpha bonded), more branched than starch

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14
Q

What is cellulose?

A

Structural component in plant cell walls (beta bonded)

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15
Q

What is Chitin?

A

Structural component in fungi cell walls and insect exoskeleton (beta bonded +nitrogen)

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16
Q

What do proteins contain?

A

Carbon, hydrogen, oxygen and nitrogen. Which are amino acids -> polypeptides/proteins are joining by peptide bonds.

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17
Q

What are amino acids?

A

Monomers of proteins

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18
Q

How many amino acids are there?

A

20

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19
Q

What are the two end terminals of each amino acid chain?

A

N-Terminus and C-Terminus

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20
Q

What does N-Terminus end with?

A

An Amino Acid

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21
Q

What does C-terminus end with?

A

Ends with the last amino acids carboxyl group

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22
Q

Describe the Primary structure of a protein structure

A

Sequence of amino acids

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23
Q

Describe the Secondary structure of a protein structure

A

Intermolecular forces between polypeptide backbone due to hydrogen bonding, forms a-helices and b-pleated

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24
Q

Describe the Tertiary structure of a protein structure

A

3-D structure, create hydrophobic and hydrophilic , sulfide bonds

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25
Q

Describe Quaternary structure of a protein structure

A

Multiple polypeptide chains come together to form one protein

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26
Q

Classifications of proteins

A

Fibrous, globular and intermediate.
Can be simple (amino acids only)
Conjugated (amino acids plus other components)

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27
Q

What is protein denaturation?

A

Loss of protein function and higher order structures. Only the primary structure is unaffected so the sequence of amino acids.

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28
Q

What are reasons for protein denaturation?

A

High/low temps, pH changes, salt concentrations

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29
Q

Function of Storage in proteins

A

Reserve of amino acids

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30
Q

Function of Hormones in proteins

A

Signaling molecules that circulate through the body to regulate physiological processes

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31
Q

Function of Receptors in proteins

A

Protein in cell membranes, bind to signal molecules to trigger charges

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32
Q

Function of Motion in proteins

A

Movement generation for cell or whole organisms

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33
Q

Function of Structure in proteins

A

Provide strength and support to tissues

34
Q

Function of Immunity in proteins

A

Prevention and protection against foreign invaders

35
Q

Function of Enzymes in proteins

A

Biological catalysts binding to substrates converting to products. Most enzymes are proteins.

36
Q

What are catalysts?

A

Increase reaction rates by lowering activation energy and reduce transition state. Do not shift chemical reaction or affect spontaneity.

37
Q

What is a transition state?

A

The unstable intermediate between reactants and products.

38
Q

Define specificity constant

A

Measures how efficient an enzyme is at binding to the substrate and converting to product

39
Q

What is the induced fit theory?

A

Active site molds itself and changes shape to fit the substrate when it binds

40
Q

What is ribozyme?

A

Is an RNA molecule that can act as enzyme (nonprotein)

41
Q

What is a cofactor?

A

Is a nonprotein molecule that helps enzymes perform reactions

42
Q

What two types of cofactors are there?

A

Organic (vitamins)

Inorganic (Metal ions)

43
Q

What are Moloenzymes?

A

Enzymes bound to cofactors (tightly bound, prosthetic groups)

44
Q

What are apoenzymes?

A

Enzymes not bound to their cofactors

45
Q

What is competitive inhibition?

A

When a competitive inhibitor directly competes with the substrate for active binding site

46
Q

How can we increase enzyme action?

A

By adding more substrate

47
Q

What is noncompetitive inhibition?

A

The noncompetitive inhibitor binds to an allosteric site, modifying the active site. The allosteric site is different than the active site. Enzyme action cannot be increased.

48
Q

How does the competitive inhibition look on the enzyme kinetics plot?

A

Km increases while Vmax stays the same

49
Q

How does the noncompetitive inhibition look on the enzyme kinetics plot?

A

Km stays the same while Vmax decreases

50
Q

What are lipids?

A

Contain carbon, hydrogen, and oxygen. (Carbohydrates) Have long hydrocarbon tails = hydrophobic.

51
Q

What do Triglycerol - lipids consist of?

A

With glycerol backbone. Glycerol + three fatty acids connected by ester linkages.

52
Q

What makes a chain saturated?

A

Has no double bonds, tightly packed (solid at room temp)

53
Q

What makes a chain unsaturated?

A

Have double bonds

54
Q

What do Cis-unsaturated fatty acids have?

A

Have kinks that cause the hydrocarbon tails to bend they do no pack tightly

55
Q

What do Trans-unsaturated fatty acids have?

A

Have straighter hydrocarbon tails that pack tightly together

56
Q

What do phospholipids consist of?

A

glycerol backbone, one phosphate group (polar), two fatty acids (nonpolar) which cause to be amphipathic

57
Q

What does amphipathic mean?

A

Hydrophilic and hydrophobic

58
Q

What is cholesterol?

A

Lipid molecule, amphipathic, most common precursor of steroid hormone, vitamin D and bile acids

59
Q

How does temperature affect membrane fluidity?

A

High-temperature increases fluidity, low-temperature decrease fluidity.

60
Q

How does cholesterol affect membrane fluidity?

A

Cholesterol holds the membrane together at high temperature and keeps membrane fluid down at low temperatures.

61
Q

Describe saturated fatty acids

A

Pack more tightly

62
Q

Describe unsaturated fatty acids

A

Less packed, have double bonds and introduce kinks

63
Q

What do Lipoproteins do?

A

Allow the transport of lipid molecules in the bloodstream due to an outer coat of phospholipids, cholesterol, and proteins.

64
Q

What are low-density lipoproteins?

A

Bad cholesterol and vessel blockage can occur leading to heart disease. Will deliver to peripheral tissue.

65
Q

What are high-density lipoproteins?

A

High protein density takes cholesterol away from peripheral tissues, good cholesterol is sent to the liver to make bile.

66
Q

What are waxes?

A

Simple lipids that have long fatty acids connected to mono hydroxyl alcohols. Used mainly as a hydrophobic protective coating.

67
Q

What are carotenoids?

A

Function as pigments. Long-chain conjugated with double bonds and six-membered rings at each end.

68
Q

What are the nucleic acids?

A

Contain nitrogen, oxygen, phosphorus, hydrogen, carbon. Contain nucleotide that builds into DNA and RNA.

69
Q

What are nucleosides?

A

Five carbon sugar and a nitrogenous base

70
Q

What do nucleotides contain?

A

Contain a phosphate group plus five-carbon sugar and a nitrogenous base.

71
Q

What does deoxyribose contain?

A

In DNA contain hydrogen at 2 carbon

72
Q

Where are ribose located?

A

In hydroxyl group at 2’carbon

73
Q

Nucleotides in DNA and RNA

A

Adenine, Thymine, Cytosine, Guanine. Uracil replaces thymine in RNA.

74
Q

What are Purines?

A

Two rings; Pur As Gold = Purines are Adenine and Guanine

75
Q

What are Pyrimidines?

A

One ring; CUT the Py = Cytosine, Uracil and thymine are pyrmindines.

76
Q

Phosphodiester bonds do what?

A

Connect phosphate group of one nucleotide at 5’carbon to hydroxyl group of another nucleotide at 3’

77
Q

DNA strands and transcription

A

Antiparallel double helix, two complementary strands with opposite directionalities.
A-T
G-C

78
Q

RNA strand and transcription

A

Single-stranded.
A-U
G-C

79
Q

How is genetic information passed down?

A

Through DNA

80
Q

What is Modern Cell theory?

A

All life forms have one or more cells.
All cells come from other cells
metabolism and biochemistry occurs within cells
all cells have the same chemical composition within similar species
organism activity is dependent on total activity.

81
Q

What is the central dogma of genetics?

A

Information passed from DNA to RNA to proteins

82
Q

What is RNA world hypothesis?

A

RNA dominated Earth.
RNA developed self-replicating and could later catalyze reactions such as protein synthesis.
RNA is reactive and unstable, DNA became a better way

DAT Prep (2 decks)

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