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B1- BIOLOGICAL MOLECULES > 1.6- PROTEINS > Flashcards

1.6- PROTEINS Flashcards

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Organic Chemistry 101 flashcards
1
Q

What is the size of proteins usually?

A

usually very large molecules

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2
Q

How are the types of carbohydrates and lipids in all organisms in terms of number + structure?

A

relatively few and they are very similar

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3
Q

Something about the shape of proteins in comparison to each other?

A

shape of any one type of protein molecule differs from that of all other types of proteins

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4
Q

How significant are proteins in living organisms?

A

very important

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5
Q

What does the word “protein” mean in greek?

A

“of first importance”

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6
Q

How involved are enzymes?

A

enzymes involved in almost every living process

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7
Q

What is amino acids used as?

A

basic monomer units which combine to make up a polymer

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8
Q

What is the name of the polymer made up of amino acids?

A

polypeptide

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9
Q

When polypeptides are combined what do they form?

A

proteins

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10
Q

About how many amino acids have been identified?

A

about 100 amino acids

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11
Q

How many amino acids occur naturally in proteins?

A

20

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12
Q

What does the fact that the same 20 amino acids occur in all living organisms provide indirect evidence for?

A

evolution

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13
Q

What does every amino acid have?

A

a central carbon atom to which are attached four different chemical group

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14
Q

What are the four different chemical groups attached to the carbon in an amino acid?

A

-NH₂
-COOH
-H
R group

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15
Q

Through what process do amino acid monomers combine to form a dipeptide?

A

condensation reaction

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16
Q

How is the water formed in the condensation reaction between amino acids?

A

combining an -OH from carboxyl group of one amino acid with -H from amino group of another amino acid

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17
Q

How do the two amino acids become linked?

A

by a peptide bond

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18
Q

Where is the peptide bond between?

A

between the carbon atom of one amino acid and nitrogen atom of other

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19
Q

How can a peptide bond of a dipeptide bond be broken and what is left?

A

through hydrolysis to give two constituent amino acids

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20
Q

What is the process called when a series of condensation reactions happen, joining many amino acid monomers?

A

polymerisation

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21
Q

What is the resulting chain of many hundreds of amino acids called?

A

polypeptide

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22
Q

What is the primary structure of any protein?

A

sequence of amino acids in polypeptide chain

23
Q

How is the sequence of amino acids in a polypeptide chain determined?

A

determined by DNA

24
Q

How is there a limitless number of primary protein structures?

A

as polypeptides have many (usually hundreds) of the 20 naturally occurring amino acids joined in different sequences, there’s a limitless number of combinations

25
Q

What does the primary structure determine?

A

its ultimate shape and hence its function

26
Q

What can a change in a single amino acid in the primary sequence lead to?

A

lead to a change in the shape of protein + may stop it from carrying out function

27
Q

What is the protein’s shape very specific to?

A

its function

28
Q

What can happen if the shape of a protein is changed?

A

it will function less well or differently

29
Q

What may a simple protein consist of?

A

consist of a single polypeptide chain

30
Q

More commonly, what does a protein consist of?

A

made up of a number of polypeptide chains

31
Q

What does the linked amino acids that make up a polypeptide possess?

A

-NH and -C=O groups on either side of peptide bond

32
Q

What overall charge does the hydrogen on -NH have?

A

an overall positive charge

33
Q

What overall charge does the O of -C=O group have?

A

overall negative charge

34
Q

Due to the charge of the hydrogen on -NH and charge of O on -C=OH what happens?

A

readily form weak bonds called hydrogen bonds

35
Q

What does the hydrogen bond between the O and H cause?

A

the long polypeptide chain to be twisted into a 3D shape

36
Q

What can the 3D shape?

A

alpha helix or beta pleated sheets

37
Q

What happens in the tertiary structure?

A

secondary protein structure can be twisted and folded even more

38
Q

What does the further folding and twisting produce?

A

gives a complex, and often specific 3D structure of each protein

39
Q

How is the tertiary structure maintained?

A

by a number of different bonds

40
Q

How is where the bonds in the tertiary structure determined?

A

depends on the primary structure of protein

41
Q

What are the bonds in the tertiary structure?(3)

A

disulfide bridges
ionic bonds
hydrogen bonds

42
Q

How strong are disulfide bridges?

A

fairly strong so not easily broken

43
Q

Where are ionic bonds formed?

A

Formed between any carboxyl and amino groups that are not involved in forming peptide bonds

44
Q

How strong are ionic bonds and how are they broken?

A

weaker than disulfide bonds and easily broken by change in pH

45
Q

How strong are hydrogen bonds + numbers?

A

numerous but easily broken

46
Q

What is important for the function of protein?

A

3D shape of protein

47
Q

What does the 3D shape allow?

A

makes each protein distinctive and allows it to recognise, and be recognised by other molecules

48
Q

What does proteins being able to interact with other molecules enable?

A

it can interact with them in a very specific way

49
Q

What do large proteins often form?

A

form complex molecules containing a number of individual polypeptide chains that are linked in various ways

50
Q

What other groups may also be associated with the molecules in the quaternary structure?

A

non-protein (prosthetic) groups

51
Q

Example of prosthetic group on protein?

A

iron-containing haem group in haemoglobin

52
Q

What determines the 3D structure in the first place?

A

the sequence of amino acids (primary structure)

53
Q

What is the most reliable test for proteins?

A

Biuret test

54
Q

What does the Biuret test detect?

A

peptide bonds

B1- BIOLOGICAL MOLECULES (10 decks)

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