Week 2 Flashcards

1
Q

Nucleic acids

A

Polymers that store, transmit and express genetic info

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2
Q

How genetic info is stored

A

Encoded in the sequences of monomers

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3
Q

2 types of nucleic acid

A

DNA

RNA

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4
Q

DNA function

A

Stores and transmits genetic info

Used to specify the amino acid sequences of proteins

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5
Q

RNA role

A

Certain specialised RNA play role in metabolism

Uses DNA info to specify the amino acid sequences

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6
Q

Nucleotide makeup

A

Nitrogen containing base
Pentose sugar
One to theee phosphate groups

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7
Q

Pyrimidines

A

Cytosine
Thymine
Uracil

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8
Q

Purines

A

Adenine

Guanine

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9
Q

Pyrimidine makeup

A

Six membered single ring

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10
Q

Purine makeup

A

Fused double ring structure

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11
Q

Phosphodiester bond

A

When the pentose sugar of the old chain and phosphate of the new chain undergo condensation reaction

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12
Q

DNA bases

A

Adenine
Guanine
Thymine
Cytosine

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13
Q

RNA bases

A

Adenine
Guanine
Cytosine
Uracil

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14
Q

Dhow base pairs are held together

A

Hydrogen bonds

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15
Q

Hydrogen bond strength

A

Relatively weak by cause there are so many provide considerable amount of force

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16
Q

Hydrogen bond - breaking

A

Not as strong as multiple covalent bonds so base pairs are easy to separate with modest energy

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17
Q

RNA makeup

A

Single strand
Many single stranded fold up to 3D
Folds back to form double stranded helix

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18
Q

RNA folding - outcome

A

3D surface for bonding and recognition of other molecules

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19
Q

DNA makeup

A

Double strand
2 separate polynucleotides that run in opposite directions
Form ladder that twists into double helix
Sugar phosphate groups form side and bases form rungs on inside

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20
Q

Ways of DNA reproduction

A

DNA replication

Transcription

21
Q

DNA replication

A

Replicated by polymerisation using existing strand as base pair template

22
Q

Transcription

A

DNA copied into rna

23
Q

Translation

A

Nucleotide sequences in most rna can be used to specify sequences of amino acids in proteins

24
Q

Enzymes

A

Catalyse biochemical reactions

25
Defensive proteins
Recognise and respond to substances that invade the organism
26
Hormonal and regulatory proteins
Control physiological processes
27
Receptor proteins
Receive and respond to molecular signals from inside and outside organism
28
Storage proteins
Store chemical building blocks for later use
29
Structural proteins
Provide physical stability and enable movement
30
Transport proteins
Carry substances within organism
31
Genetic regulatory proteins
Regulate when, how and to what extent a gene is expressed
32
Functional groups of amino acids
Nitrogen containing amino group | Carboxyl group
33
Peptides
Amino acid polymers of 20
34
Polypeptide formation
Via the sequential addition of new amino acids to the end of existing chains The amino group of the new amino reacts with the carboxyl group of the end amino to form peptide bond
35
Primary structure of proteins
Established by covalent bonds
36
Protein secondary structure
Regular repeated spatial patterns
37
Secondary structure - alpha helix
Right handed coil that turns in same direction | R groups extend outward from peptide backbone
38
Secondary structure- beta pleated sheet
Two or more sequences are extended and aligned | Stablilised by hydrogen bonds
39
Protein structure - tertiary
Bent a specific sites and folded back and forth | Definite 3D shape
40
Tertiary proteins - exposed surface
Resent functional groups capable of interacting with other molecules in the cell
41
What determines tertiary structure
Interactions between r groups
42
What determines secondary structure
Hydrogen bonding between n-h and c=o groups within and between chains
43
What changes protein structure
Environment | Interactions with other molecules
44
Environmental conditions that affect protein
Increase in temp Concentration of h+ High concentrations of polar substances Non polar substances
45
Enzyme function
Lowers activation energy by enabling reactants to come together and react easily
46
Active site
Where substrate bind to the enzyme
47
Competitive inhibitor
Inhibitor and substrate compete only one can bind to the active site
48
Non competitive inhibitor
Bonds to a site away from active site, changing the enzymes shape so the subrate can no longer fit