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Biology > Topic 2 Wood > Flashcards

Topic 2 Wood Flashcards

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1
Q

Amino acids molecules

A
  • carbon
  • oxygen
  • hydrogen
  • nitrogen
  • sulphur (only 2 of them)
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2
Q

Structural protein

A

tendons, cartilage, hair, nails

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3
Q

Contractile protein

A

muscles

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4
Q

transport protein

A

haemoglobin

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5
Q

storage protein

A

milk

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6
Q

hormonal protein

A

insulin, growth hormones

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7
Q

enzyme protein

A

catalyses reactions in cells

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8
Q

protection protein

A

immune response

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9
Q

What are proteins used for?

A
  • catalysis: catalyzing the breakdown of products
  • transport: some proteins transport various substances
  • information transfer: for example hormones
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10
Q

Where does the bond form between amino acids?

A

between the carboxyl and amino group

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11
Q

How are two amino acids joined together?

A

in a condensation reaction, removing water and forming peptide bonds (add water in hydrolysis to reverse)

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12
Q

Primary structure of a protein

A

the sequence of amino acids joined together to form a polypeptide chain

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13
Q

What does the shape of a protein determine?

A

its function

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14
Q

Amino acids are soluble in water

A
  • they form ions in solution as a hydrogen ion leaves the carboxyl group and a hydrogen ion joins the amine group
  • this means the molecule becomes dipolar (with the amine group positive)
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15
Q

Secondary structure of a protein

A

localized 3D shape formed by a polypeptide chain e.g. alpha helix or beta pleated sheet (only hydrogen bonds)

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16
Q

Tertiary structure of a protein

A

Overall compact 3D shape formed by a fully folded polypeptide. Multiple bonds: hydrophilic/phobic interactions, disulphide bridges, ionic, hydrogen

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17
Q

Quarternary structure of a protein

A

combination of different polypeptide chains and sometimes non-protein groups

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18
Q

Alpha helix

A

coiled, corkscrew shape held by hydrogen bonds

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19
Q

beta pleated sheet

A

folded, held side by side

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20
Q

Hydrophilic/phobic interactions

A

trap water in 3D shape

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21
Q

disulphide bridge

A

bond between two sulphurs (only in two amino acids)

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22
Q

Ionic bond

A

bond between charged molecules

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23
Q

van der Waales forces of attraction

A

block between CH3

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24
Q

Two groups proteins can be split into:

A

globular - blob shape and fibrous - thin shape line

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25
Q

Globular proteins

A
  • folded into a compact spherical shape
  • are soluble due to hydrophilic side chains that project from the outside of the molecule
  • 3D shape is crucial in ability to form enzyme-substrate complex and catalyse reactions within cells
  • 3D shape critical in roles in binding to other substances (e.g. antibodies, enzymes, insulin)
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26
Q

Fibrous proteins

A
  • remain as long chains
  • several polypeptide chains can be cross-linked for extra strength
  • are important structural molecules (e.g. hair skin collagen, tendons, bones, cartilage)
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27
Q

What type of protein are enzymes?

A

globular proteins

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28
Q

What reactions does an enzyme speed up?

A

both anabolic (building up) and catabolic (breaking down) reactions but not reactions that otherwise wouldn’t occur

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29
Q

How do enzymes work?

A

they lower the activation energy required for the reaction to occur

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30
Q

Key features of an enzyme:

A
  • don’t get used up
  • the active site is where the substrate binds to
  • many enzymes are specific to just one reaction
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31
Q

Lock and key theory

A
  • various substrate molecules approach the enzyme’s active site
  • only one with a specific shape will fit
  • this binds to the active site forming an enzyme-substrate complex
  • the enzyme catalyses the reaction either breaking bonds or making them
  • then the products are released
32
Q

Features of the lock and key theory

A
  • lowers the activation energy
  • still there at the end (doesn’t get used up)
  • only one reaction can occur at a time as only one enzyme-substrate complex can be formed at a time
33
Q

Induced fit theory

A
  • substrate molecule moves into the active site (only needs to be a similar shape)
  • forces between the two molecules distorting the enzyme and its active site so it tightly envelopes the substrate
  • enzyme-substrate complex is formed
  • breaks down/builds up
  • leaves
  • enzyme springs back into shape
34
Q

Enzyme

A

biological catalyst

35
Q

Biological catalyst

A

globular protein that speeds up a reaction by lowering the activation energy

36
Q

activation energy

A

energy required to start a reaction

37
Q

active site

A

where the enzyme-substrate complex forms and the reaction occurs

38
Q

enzyme-substrate comlpex

A

where the substrate binds to the active site

39
Q

lock and key theory definition

A

the substrate fits exactly into the active site

40
Q

induced fit theory definition

A

substrate forces its way into the active site

41
Q

Factors affecting the rate of reaction:

A
  • temperature –> bonds break, change active site shape, can’t bind, no reaction
  • pH
  • enzyme concentration –> increase rate of reaction
  • substrate concentration
42
Q

Competitive enzyme inhibitors

A
  • active site directed

- all heading for active site,different substrate goes to active site, slows down doesn’t stop

43
Q

Non-competitive inhibitors

A
  • non-active site directed
  • binds to elsewhere on enzyme, active site changes shape, no reaction can occur
  • when removed goes back to normal
44
Q

Enzyme inhibitors

A
  • can be either reversible or irreversible

- can be competitive or non-competitive

45
Q

DNA

A

deoxyribose nucleic acid (without oxygen/lacking)

46
Q

RNA

A

ribose nucleic acid

47
Q

Nucleoside

A
  • (pentose) sugar + nitrogenous base

- formed in a condensation reaction

48
Q

Nucleotide

A
  • nucleoside (sugar + nitrogenous base) +phosphoric acid

- formed in a condensation reaction

49
Q

What is the bond between a phosphate group and sugar called?

A

phosphoester bond

50
Q

Name the four nitrogen bases

A
  • adenine
  • thymine (in RNA uracil is used instead)
  • cytosine
  • guanine
51
Q

Purine base

A

2 carbon rings e.g. adenine and guanine

52
Q

Pyrimidine base

A

1 carbon rings e.g thymine, cytosine and uracil

53
Q

Which bases are matched together

A
  • adenine and thymine (2 hydrogen bonds)

- cytosine and guanine (3 hydrogen bonds)

54
Q

5 prime end: carbon 5 at the top

A

will have a 3 prime end: carbon 3 at the other end

55
Q

Opposite strand 3’ end at top

A

will have a 5’ end at bottom –> strands run antiparallel

56
Q

How is DNA packaged

A
  • DNA is wrapped around histone proteins
  • These histone proteins are packaged together into octaves (groups of eight)
  • This forms chromatin which in turn forms chromosomes
57
Q

Gene

A

sequence of bases on a DNA molecule coding for a sequence of amino acids in a polypeptide chain

58
Q

Locus

A

position on a chromosome

59
Q

Triplet code

A

is degenerate which means that each amino acid is coded for by more than one triplet/amino acid

60
Q

Sequence of bases in DNA tells…

A

the cell which amino acids link together to make a protein

61
Q

RNA is…

A

single stranded

62
Q

DNA is…

A

double stranded

63
Q

Why is DNA being double stranded an issue?

A

because it can’t leave the nucleus but it needs to get the information to the cytoplasm

64
Q

Where can you find most DNA?

A

in the nucleus

65
Q

What does DNA contain?

A

information/code that determines the cell structure and function by telling the cell which proteins to make

66
Q

How does RNA leave the nucleus?

A

through a nuclear pore

67
Q

What are the 3 types of RNA involved in protein synthesis?

A
  • mRNA (messenger)
  • tRNA (transfer)
  • rRNA (ribosomal)
68
Q

Transcription summary

A
  • DNA unwinds

- DNA is copied into mRNA which can then leave the nucleus through a nuclear pore

69
Q

Translation summary

A
  • mRNA passes through the ribosome
  • tRNA brings the amino acids to the ribosome and temporarily bonds to the mRNA
  • the codon and anticodon match up
  • This codes for a protein before the tRNA leaves and the next protein is translated
  • this creates a polypeptide chain
70
Q

Conservative DNA replication

A
  • new strands of DNA form alongside existing double helix

- one double helix has parents, one is new

71
Q

Semi-conservative DNA replication

A
  • DNA unzips (proteins and enzymes involved) and new nucleotides form alongside each strand
  • one parent strand, one new strand for each double helix
72
Q

Dispersive DNA replication

A
  • DNA completely breaks down then reforms using pre-existing and new nucleotides
  • both double helixes are mixed and matched
73
Q

How does DNA replicate?

A

by a semi-conservative method

74
Q

Replication fork

A

the point at which the two strands are separated

75
Q

Leading strand

A

runs in a 5’ to 3’ direction, replicated continuosly

76
Q

Lagging strand

A

runs in a 3’ to 5’ direction, replicated discontinuosly

77
Q

Two strands of DNA run in…

A

an antiparallel direction. Each strand is replicated in the same way

Biology (14 decks)

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