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Unit 1.1 Biology AS Level 🌺 > proteins > Flashcards

proteins Flashcards

1
Q

what is the amino group

A

h - n - h

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1
Q

what is carboxyl group

A

o = c - oh

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2
Q

How is protein different from carbohydrates and lipids

A

also have nitrogen atoms

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3
Q

defenition of protein

A

polymers made of amino acids monomers

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4
Q

what is a chain of amino acids called

A

polypeptide

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5
Q

what does the shape of proteins depend on?

A

specific sequence of amino acids in the chain

shape determins its function

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6
Q

how many ‘sections’ are in the protein diagram

A

4

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7
Q

what are the ‘sections’ are in a protein diagram

A

amino group - n h2
carboxyl group - cooh
hydrogen atom
r group

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8
Q

what is the r group

A

variable group of atoms

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9
Q

simplest amino acid is

A

glycine

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10
Q

what is a R group of a amino acid

A

variable group of atoms

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11
Q

what is a R group of a fatty acid

A

long hydrocarbon chain

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12
Q

what are essential amino acids

A

cannot be syntheised by our bodies - must be provided by diet

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13
Q

what are non essential amino acids

A

can be synthesised by our own bodies

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14
Q

how are 2 amino acids joined

A

amino group of one reacts with the carboxyl group by condensation reaction

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15
Q

how are 2 amino acids joined (in terms of bonding)

A

water is elimated and peptide bond is formed

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16
Q

peptide bond definition

A

chemical bond formed as amino group reacts with the carboxyl group of another by condensation reaction

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17
Q

example of a quaternary protein

A

haemoglobin

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18
Q

example of tertiary protein

19
Q

what is the primary structure

A

sequence of amino acids in a polypeptide chain

20
Q

what is the sequence of amino acids determined by

A

one gene codes for one polypeptide

21
Q

in primary protein what is the bond

22
Q

what are secondary protein structures

A

shape that the polypeptide chain forms due to hydrogen bonding

23
Q

what affect does hydrogen bonding have on secondary protein structures

A

twist and folds polypeptide forming alpha helix or beta pleated sheet

24
Q

what extra bonds are present in secondary

25
Q

how are tertiary protein structure created

A

alpha helix is further folded and twisted to give a more complec compact 3D structure

26
Q

what extra bonds are present in tertiary

A

disulphide, ionic, covalent ,hydrophobic

27
Q

how are quaternary protein structure formed

A

combination of 2 or more polypeptide chains in tertiary form

28
Q

what are quaternary protein

A

assosciated with non - protein groups and form large compex molecules such as haemoglobin

29
Q

how many chains does haemoglobin have

A

4 polypeptide

30
Q

what are the 2 different classifications of proteins

A

globular
fibrous

31
Q

globular proteins functions

A

enzymes, antibodies and hormones

32
Q

how are globular proteins structure

A

compact and folded into a 3d spherical molecule

33
Q

are globular proteins soluble in water

34
Q

what do fibrous proteins do

A

perform structural functions

35
Q

structure of fibrous proteins

A

consists of polypeptides in parallel chains or sheets to form long fibres

36
Q

properties of fibrous proteins

A

insoluble in water, strong and tough

37
Q

how many polpeptide chains does collagen have

38
Q

example of fibrous protein

39
Q

example of globular protein

A

haemoglobin

40
Q

are polypeptide chains in haemoglobin same or different

41
Q

are polypeptide chains in collagen same or different

42
Q

are haemoglobin assosciated with non protein groups

A

yes - iron

43
Q

highest level of protein structure for haemoglobin

A

quaternary

44
Q

highest level of protein structure for collagen

45
Q

science of biuret test

A

in presence of peptides - copper 2 ion forms violet complex in an alkaline solution

46
Q

fatty acid test description

A

add 1ml of absolute ethanol - forms white emulsion

Unit 1.1 Biology AS Level 🌺 (8 decks)

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