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BIOL 2410 > Lecture 2: Biomolecules > Flashcards

Lecture 2: Biomolecules Flashcards

1
Q

What are biomolecules?

A

Biomolecules are an organic molecule that is commonly associated with life

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2
Q

Define organic molecule

A

contains carbon

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3
Q

What is the general

Formula of Carbohydrates?

A

C(n) H(2n) O(n)

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4
Q

Are most carbohydrates Hydrophilic or Hydrophobic

A

Hydrophilic

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5
Q

What are carbohydrates typically used for?

A

Structure and energy

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6
Q

Define Monosaccharides and give 2 examples

A

Are a simple sugar, five carbons or six carbon

ex; Ribose, Glucose

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7
Q

Define Disaccharides

A

Consist of Glucose and another monosaccharide

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8
Q

Define Polysaccharide

Give 2 examples

A

Are glucose polymers, all living cells store glucose for energy in this form
Ex; Cellulose and Starch

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9
Q

Nucleotides and Nucleic Acids are involved in what

A

energy metabolism and signaling

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10
Q

A nucleotide consists of what three things

A

1) One or more phosphate groups
2) A 5-carbon sugar
3) A ring structure called a nitrogenous base

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11
Q

The structure of a nitrogenous base determines whether the nucleotide is

A

Adenosine, Cytosine, Guanosine, or Thymidine

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12
Q

Define ATP

A

Is Adenosine Triphosphate which is the basic molecule of energy storage in most mammals and organisms

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13
Q

Adenosine is a

A

Neurotransmitter

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14
Q

Define GTP

A

Is Guanosine Triphosphate which is an energy source in physiological chemical reactions

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15
Q

Define cAMP

What enzyme converts ATP to cAMP

A

An important signaling molecule within cell

Adenyly cyclase

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16
Q

Define cGMP

What enzyme converts GTP to cGMP

A

An important signaling molecule within the cell

Guanylyl cyclase

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17
Q

Lipids contain

A

Mostly carbon, hydrogen, few oxygen, nitrogen and phosphorus

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18
Q

Are lipids typically hydrophilic or hydrophobic molecules

A

Hydrophobic or have hydrophobic parts

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19
Q

What are the 5 groups of Lipids?

A

1) Fatty acids
2) Glycerides
3) Phospholipids and Sphingolipids
4) Steroids
5) Eicosanoids

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20
Q

Fatty acid properties are

A

a long chain with 8-28 carbon atoms bound to hydrogen with a carbonyl functional group

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21
Q

Saturated fatty acide have ____ bonds and a ____ chain and are ____ at room temp

A

no double bonds , straight solid

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22
Q

Unsaturated fatty acids have ______ bonds and a _____ chain and are ____ at room temp

A

double bonds, kinked, liquid

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23
Q

What are the 3 roles of lipids

A

1) Structure of cell
2) Energy source
3) Communication both within and between cells

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24
Q

Glycerides are a derivative or what

A

derivative of Fatty acids

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25
Q

Glycerides typically do what to water

A

takes it out

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26
Q

What are the three kinds of glycerides

A

Mono-
Diglyceride
Tri-

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27
Q

Phospholipids and Sphingolipids contain

A

a phosphate group, a diglyceride and an R group

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28
Q

Phospholipids are _____ molecules that have _____ head and _____ tails

A

Amphipathic molecules with polar heads and non-polar tails

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29
Q

Define amphipathic

A

having both hydrophilic and hydrophobic molecules

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30
Q

Phospholipids come in 3 shapes what are they

A

Bilayer,
Micelles (droplets)
Liposomes (3D, aqueous center)

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31
Q

Phospholipids are converted to Sphingolipids by

A

removing the glycerol and changing it into sphingosine

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32
Q

Phospholipids are _____ than sphingolipids

A

smaller

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33
Q

What is the basic structure of Steroids?

A

Consists three six-carbon ring with one five carbon ring (17 carbon)
Different function group (R group)

34
Q

What two areas do steroids play a role in

A

communication and cell structure

35
Q

What are 2 examples of steroids

A

Testosterone and cortisol

36
Q

Eicosanoids consist of ____ carbons and derived from

A

20, fatty acid arachidonic acid

37
Q

Eicosanoids play a role in

A

communication within cells

38
Q

Proteins are ________ with _____ chains made up of _____

A

macromolecules , linear and amino acids

39
Q

How many amino acids are encoded by the universal genetic code; and of them how many are essential (need to be consumed)

A

20 and 9

40
Q

Amino acids can be

A

acidic, basic, polar, non-polar

41
Q

A short chain of amino acids are called _____ where as a long chain are called ____

A

Peptides; Proteins

42
Q

What are the four structures of Proteins

A

Primary
secondary
tertiary
quaternary

43
Q

Define primary structures of proteins

A

Linear sequence, 10-100 AA

44
Q

Define secondary structures of proteins

A

Covalent bond angles between amino acids. Can be a-helix or B-pleated sheets

45
Q

Define Tertiary proteins

A

A 3D shape , looks like random lines?

46
Q

Define quaternary structures of proteins

A

Muletiple subunits combined with noncovalent bonds

Can be fibrous or globular

47
Q

Give an example of a fibrous protein and a globular protein

A 
collagen = fibrous
hemoglobin = globular
48
Q

Proteins are the ____________ ___________ of cells

A

Molecular tools

49
Q

What are the 7 functional groups of proteins?

A

1) Enzymes
2) Membrane transporters
3) Signal molecules
4) Receptors
5) Binding proteins
6) Regulatory proteins
7) Immunoglobulins

50
Q

Enzymes are

A

biological catalysts, speed up chemical reactions

51
Q

Membrane transporters

A

May form channel in cell membrane or bind to molecule and carry it through a membrane

52
Q

Signal molecules

A

signal other molecules

53
Q

Receptors are proteins that

A

bind signal molecules and initiate cellular response

54
Q

Binding proteins are found and do what

give an ex

A

are mostly found in the ECF , bind and transport molecules throughout the body
ex; hemoglobin

55
Q

Immunoglobulins are also called what and do what

A

antibodies and help protect the body from foreign substances

56
Q

Define a Ligand

A

a molecule that binds to a protein binding site

57
Q

Define an Agonist ligand

A

A ligand that binds to a protein binding site and alters the state of said protein, resulting in a biological response

58
Q

Define Antagonist ligands and give the two types

A

A Ligand that reduces the action of an agonist, binds but causes no biological response
can be competitive (act to block the agonist at its binding site) or Allosteric (act to block the agonist by binding to the protein away from the binding site and inactive the binding site)

59
Q

What is another name for n antagonist ligand

A

Inhibitor

60
Q

Define affinity

A

A protein binds a ligand with affinity

high = strong

61
Q

Rate of protein binding can be modified by what 3 things

A

1) Depends on type of protein
2) ligand concentration
3) Saturation

62
Q

Define binding regulatory subunits

A

They change protein’s activity to bind a ligand, or change the proteins activity/ability to create a response

63
Q

Define Isoforms

A

Closely related proteins whose function is similar but whose affinity for ligands differ

64
Q

What can pH or temperature cause

A

Structural changes

65
Q

True or False; Phosphorylation does not mean it activates the protein?

A

True

66
Q

Describe phosphorylation

A

Adding a phosphor via the enzyme kinase

67
Q

Describe Dephosphorylating

A

Removing a phosphor via the enzyme phosphatases

68
Q

When a Phosphors is removed from ATP it turns into what and energy us _____

A

ADP and energy is released

69
Q

What is the difference between an organic molecule and a biomolecule?

A

Organic molecule is a molecule that contains carbon, biomolecules is an organic molecule that is commonly associated with life , ex carbohydrates, lipids

70
Q

Why would a cell store glucose as glycogen?

A

Because polysaccharides are glucose polymers and all living cells store glucose for energy in this form

71
Q

Structurally, what is different between a phospholipid and a sphingolipid

A

sphingolipid have a sphingosine backbone and tail with no glycerol

72
Q

Why are some fatty acids considered saturated and some considered unsaturated?

A

Saturated fatty acids = double bonds, solid at room temp

Unsaturated fatty acids = no double bonds, liquid at room temp

73
Q

What is the significance of different R-Groups

A

R groups alter amino acids

74
Q

True or False; All amino acids are considered acidic

A

False

75
Q

What does adding an antagonist do to reaction velocity?

A

Slows down the reaction because antagonist binds to a protein and decreases its activity

76
Q

What role do cofactors play in activation?

A

attaches to their protein before the binding site will become active and bind to ligand

77
Q

Describe chemical modulators

A

Molecules that bind covalently or non covalently to a protein and alter their binding ability or their activity

78
Q

Describe irreversible antagonists

A

compete with the customary ligand for binding sites

79
Q

Allosteric modulators

A

bind reversibility to protein at regulatory site away from the binding site, by changing the shape at the binding site

80
Q

Define and distinguish between the processes of up-regulation and down- regulation

A 
Down-Regulation = removal of proteins
Up-Regulation = production of new proteins
81
Q

Define saturation and describe how proteins can reach the point of saturation

A

saturation is when concentration of ligand exceed some point, protein molecules have no free binding site and rate reaches a max rate

BIOL 2410 (11 decks)

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