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Biology 107 > LECTURE 2 & 3 > Flashcards

LECTURE 2 & 3 Flashcards

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1
Q

The formation of covalent bonds results in an

A

arrangement of orbitals in the valence shell.

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2
Q

Weak chemical bonds:

A

these interactions can be reversible, or modified to the molecule.

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3
Q

Van der waals interactions

A

Because of random positioning of the electrons in the orbitals, net displacements can occur, creating brief charge differences. This dynamic charge distribution allows molecules to stick to each other if they are very close. Different molecules exhibit different “stickiness” depending on the arrangement of respective atoms.

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4
Q

The formation of covalent bonds results in

A

Rearrangement of orbitals in the valence shell.

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5
Q

The change in _______ forms the bond

A

Charge

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6
Q

Weak chemical bonds are

A

Are reversible and modified by changes.

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7
Q

The four properties of polar water molecules

A

1) cohesion of water molecules

2) moderation of temperature by water
- heat of vaporization
- Ava-oration cooling: as water evaporates from surface, remaining liquid cools.

3) water (solids) is less dense then water (liquid)

4) water is important solvent
- hydrophilic
- hydrophobic

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8
Q

The three types of isomers

A

1) structural isomers
2) geometric isomers
3) enantiomers

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9
Q

Structural isomers

A

Can have a different bond order of atoms

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10
Q

Geometric isomers

A

Cis VS trans isomers

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11
Q

Enantiomers

A

When 4 different atoms ( groups or atoms) bond to carbon, an asymmetric arrangement occurs.

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12
Q

How do you know if something is an Enantiomer?

A

If the two molecules are mirror images, and cannot be superimposed on each other, they are enantiomers.

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13
Q

Macromolecules

A

Large molecules that make up living cells

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14
Q

The four types of macromolecules

A
  • carbohydrates
  • proteins
  • nuclei acids
  • lipids

All of which are polymers

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15
Q

Polymers form via ___________. And how?

A

Dehydration reactions (removing water, forming bonds)

They form by attaching through the formation of a covalent bond and removing the water.

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16
Q

How are. Polymers disassembled

A

Through hydrolysis (adds water into molecule, breaking bonds)

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17
Q

Adding different monomers together allows for the

A

Formation of polymers with distinct properties

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18
Q

Carbohydrates

A

Monosaccharides (one sugar)

  • added together to build disaccharides and polysaccharides
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19
Q

Monosaccharides with 3 carbons

A

Glyceraldehyde

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20
Q

Monosaccharides with 5 carbons

A

Ribose

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21
Q

Monosaccharides with 6 carbons

A

Glucose, galactose, fructose

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22
Q

How do cells extract every from glucose (monosaccharides)

A

Via cellular respiration.

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23
Q

The carbon form sugars that are broken down can be

A

Reused to form other molecules

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24
Q

Polysaccharides can be sued for

A
  • carbohydrate storage

- structural purposes

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25
Q

Disaccharide

A

Fros when a dehydration reaction joins two monosaccrhides

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26
Q

Types of Storage polysaccharides

A

1) starch (amylopectin)

2) glycogen

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27
Q

Starch

A

Glucose polymers, each monomer joined via 1-4 glycosidic linkages (alpha configuration)

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28
Q

Amylopectin

A

(Branched Starch)

Branches via alpha 1-6 linkages.

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29
Q

Amylose

A

Starch that is unchanged and helical.

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30
Q

Glycogen

A

Animal store glucose in THIS polysaccharides form, which is structurally similar to amylopectin, BUT more branches

31
Q

Steroids

A
  • they are lipids
  • carbons skeleton consisting of four rings.

( EXAMPLE: cholesterol )

32
Q

Cholesterol

A

Component in animal membranes

  • provides strength and flexibility to animal membranes.
33
Q

Proteins

A
  • proteins are polymers of amino acids
34
Q

Amino acids

A

Amino acids can exist as different enantiomers, but all proteins use L=enantiomers

35
Q

Polar side chains

A
  • glycine
  • alanine
  • valine
  • Leucine
  • isoleucine
  • methionine
  • phenylalanine
  • tryptophan
  • proline

(ALL OF THEM HYDROPHOBIC)

36
Q

Polar side chains ROPHILIC

A
  • Serine
  • Threonine
  • Cysteine
  • Tyrosine
  • Asparagine
  • Glutamine

ALL OF THEM HYDROPHILIC

37
Q

Electrically charged

A

1) acidic (negativity charged)

2) basic (positively charged)

38
Q

Acidic (negatively charged)

A
  • aspartic acid (Astarte)

- Glutamic acid (glutamate)

39
Q

Basic (positively charged)

A
  • lysine
  • arginine
  • histidine
40
Q

Amino acids are linked by

A

Peptide bonds

41
Q

A polypeptide is a polymer of

A

Amino acids

42
Q

Flour levels of protein structure

A
  • primary
  • secondary
  • tertiary
  • quaternary
43
Q

Primary structure

A

The linear sequence of amino acids.

Structure is determined by inherited genetic information.

44
Q

Poolypetides have an

A

NH3 (amino) end, and a COO- (carboxyl) end

45
Q

Secondary

A

Formation of a-helixes or B-pleated sheets due to hydrogen bonding between O of carbonyl group and the H of the amino group.

46
Q

When do B-pleated sheets form

A

When peptide sequence lie next to each other in antiparallel orientation.

47
Q

Tertiary

A

The arrangement of the peptide chain due to interactions between R groups, that gives the protein it’s distinctive shape.

(Transthyretin polypeptide)

48
Q

Quaternary

A

Results from the aggregation of two or more polypeptide subunits.

(Transthyretin & hemoglobin)

49
Q

Desaturation

A

Loss of proteins native structure

50
Q

A denatured protein is

A

Biologically inactive.

51
Q

Diseases caused by misfolded proteins

A
  • Alzheimer’s
  • Parkinson’s
  • mad cow
52
Q

Chaperonins

A

Proteins that assist proper folding of other proteins

53
Q

Steps of chaperonin actions

A

1) an unfolded polypeptide enters the cylinder from one end
2) the cap attaches, casing cylinder to change shape in such way that it creates a hydrophilic environment for the fouling of the polypeptide.
3) the cap comes off, properly folded protein emerges.

54
Q

Can a protein function if not properly folded?

A

NOO

55
Q

Nuclei acids

A

Coded information that cells transmit to further generations and determine protein production

56
Q

Two types of cyclic acids

A

Deoxyribonucleic acid (DNA)

Ribonucleic acid (RNA)

57
Q

Polynucleotide made of

A

monomers called nucleotides

58
Q

Nucleotides consist of 3 different molecules joined together

A
  • phosphate
  • 5 carbon sugar
  • nitrogenous base

(Nucleoside and nucleotide)

59
Q

RNA sugar is

A

Ribose

60
Q

DNA sugar is

A

Deoxyribose

61
Q

Features of a nucleotide

A
  • 1’ C : attaches to the base
  • 2’ C: OH in RNA “two prime OH”
    2’ C: H in DNA
  • 3’C: OH important for polymer formation: “three-prime OH”
  • 5’ C: attaches to phosphate group “five-prime phosphate”
62
Q

To types of nitrogenous bases

A

Pyramidines and purines

63
Q

Pyrimidines

A
  • cytosine
  • thymine
  • Urical
64
Q

Purines

A
  • adenine

- guanine

65
Q

Nucleotide monomers can be added together to form ______ ____ polymers via …

A

Nucleic acids … dehydration reaction

66
Q

When nucleotide monomers are added,

A

Nucleotide triphosphate is added, and two phosphates are removed when it gets added.

67
Q

What’s the backbone of DNA made of

A

Sugar-phosphate

68
Q

Phosphate groups is at the ___ end and OH group is at the ___ end

A

5’ and 3’

69
Q

Linkage between nucleotides is a

A

Phosphodiester linkage

70
Q

RNA molecules are usually a

A

Single polynucleotide chain

71
Q

Base pairing can happen between RNA and …

A
  • DNA
  • other RNA’s
  • itself
72
Q

Nucleotide acids

A

DNA and mRNA

73
Q

MRNA

A

(Messenger RNA) transmits information within the cell.

Biology 107 (21 decks)

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