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AH Biology > Unit 1.2c(i) > Flashcards

Unit 1.2c(i) Flashcards

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1
Q

What are some examples of what proteins function as?

A
  • enzymes
  • hormones
  • antibodies
  • regulators
  • transporters
  • structural proteins (form skin, hair etc)
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2
Q

What do polymers of amino acids make?

A

Monomoers

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3
Q

How many amino acids are there?

A

20

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4
Q

What does amino acid structure determine?

A

Proteins structure

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5
Q

What are R-groups?

A

Amino acid side groups

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6
Q

Do all R groups have the same functional groups?

A

No they all have different functional groups

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7
Q

What are the 4 groups that amino acids R groups fall into?

A
  • Basic (+ charge)
  • Acidic (- charge)
  • Polar
  • Hydrophobic
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8
Q

What are R group’s important for?

A

The protein function

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9
Q

What gives amino acids their unique chemical properties and their specific shapes?

A

R groups

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10
Q

What determines how proteins fold and interact?

A

R groups

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11
Q

What do basic r-groups have?

A

NH2

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12
Q

If the r-group is basic what can it accept and why?

A

It accepts H+/protons because of its NH2 becoming NH3+

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13
Q

Why would basic r groups become hydrophilic?

A

If they accept a proton

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14
Q

What group do acidic R groups have?

A

They have carboxylic acidic groups, COOH

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15
Q

Do acidic R groups gain or donate proteins/H+ ions?

A

They donate to other atoms

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16
Q

What is formed when acidic r groups donate a proton?

A

The become COO-

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17
Q

What halogens to acidic r groups when they donate a proton?

A

They become negatively charged and strongly hydrophilic

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18
Q

Are polar r groups hydrophilic or hydrophobic?

A

Hydrophilic

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19
Q

Why are polar r groups hydrophilic?

A

They form weak hydrogen bonds with water molecules

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20
Q

Why do polar R groups look for water contact?

A

They have a more positive and negative side

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21
Q

What do polar groups have on the side of their r side chains?

A

Oxygen, nitrogen and sulfur

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22
Q

What is the simplest of amino acid r groups?

A

Hydrophobic

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23
Q

What do hydrophobic R groups not contain?

A

OH, COOH, NH2, SH

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23
Q

Is hydrophobic polar or non polar?

A

Non polar

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24
Do hydrophobic R groups ever develop a charge?
They don’t become charged
25
Is hydrophobic water loving or water hating?
Water hating
26
What are the 4 levels of proteins?
Primary, Secondary, Tertiary, Quaternary
27
What is the primary amino acid structure?
The order in which amino acids are synthesised during translation into the polypeptide
28
What do peptide bonds do?
They join the amino acids together that make the protein
29
How are peptide bonds formed?
Condensation reactions between carboxylic groups and amine groups on neighbouring amino acids
30
What does the carboxylic acid loose when it makes a condensation reaction?
OH
31
What does the amine group lose in a condensation reaction?
H
32
How is the amino acid group extended?
By the continuous addition onto the end of the chain
33
What is the amine end and the carboxylic acid end called?
The N and C terminus
34
What are amino acid names represented by?
Their 3 letter abbreviations
35
What forms the secondary structures?
Hydrogen backbones
36
What are the secondary structures called?
- a-helices - parallel, antiparallel B-sheets, or turns
37
How do secondary structure 3-d shaped form?
The backbone folds
38
What does an a-helix secondary structure look like?
Spirals
39
What sticks out the the a-helix?
R-groups stick out
40
Why do a-helix’s form their specific shape?
Because hydrogen bonds form between the 4th peptides (between oxygen of carboxy and hydrogen of the amine)
41
How are the peptide bonds formed in the a-helix?
The weak positive hydrogen is attracted to the weak negative oxygen
42
How many amino acids are in each turn of the a-helix turn?
3.6
43
How many amino acids are in a typical section of an a-helix?
11 amino acids
44
Why are the R-groups free to interact?
Because they face outwards
45
How are beta pleated sheets formed?
Hydrogen bonds form between parts of the polypeptide stands running next to each other
46
Are the hydrogen-oxygen bonds the same as they are in the a-sheet?
Yes
47
Where do the R-groups sit on the beta pleated sheet?
Above and below
48
What direction do beta pleated sheets usually run in?
Antiparallel (opposite directions)
49
What determines how antiparallel structures run?
Where the N and C terminal are
49
What do turns do?
Reverse the polypeptide direction
50
What do turns allow?
Interactions between secondary structure elements
51
What is the tertiary structure?
The complex 3D conformation that the final polypeptide structure takes
52
What interactions establish the tertiary structures?
Interactions between amino acid R groups
53
How do prosthetic groups improve tertiary structures?
By giving an added function
54
What are the 6 interactions tertiary structures undergo?
Hydrogen Bonds Disuphilde Bridges Ionic Bonds Hydrophobic Interactions London Dispersion Forces Van de Waals Interactions
55
How is a hydrogen bond formed?
Formed by hydrogen and oxygen atoms from the main chain and R groups
56
How are disulphide bridges formed?
They’re formed if the R-groups in two amino acids contain a sulphur atom and are near each other
57
How are ionic bonds formed?
They’re formed in solutions of carboxylic acid and amino groups that form charged groups in a solution. If the charges are opposite an ionic bind will form
58
How are hydrophobic interactions formed?
They are formed when hydrophobic R groups cluster towards the interior of the protein molecule
59
What are LDFs?
They are temporary attractive forces that individually weak but collectively contribute to maintaining protein structure
60
What are van de Waals interactions?
they are electrical interactions between 2+ atoms/molecules that are very close to each other
61
Are van de Waals weak or strong interactions?
They are both; Weak by themselves Strong when working together
62
Wha quaternary structures?
They are several connected polypeptide sub-units that exist in proteins and are held together by tertiary interactions
63
What happens if a protein only contains 1 polypeptide subunit?
No quaternary structure it formed, it stops at the tertiary structure.
64
Haemoglobin in a quaternary structure, how many polypeptide subunits is it made of?
4
65
Are prosthetic groups added to quaternary structures?
Yes they are
66
Wha are prosthetic groups?
They are additional non-protein structures with no necessary functions
67
What’s an example of a non-prosthetic group and where can it be found?
Haem found in Haemoglobin
68
What does Haem contain?
An iron atom for oxygen binding
69
How is iron bound to Haemoglobin?
It is covalently bound due to histidine amino acids
70
What are the two main factors that impact protein structure?
Temperature and pH
71
What happens to a protein when it denatures?
It looses its shape and function
72
What influences R-group interactions?
Temperature and pH
73
What is impacted when temperature increases?
First weak then strong covalent bonds are disrupted
74
What does the alteration of pH from optimum result in?
The ionic intercations between R-groups becoming lost

AH Biology (51 decks)

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