Proteins Flashcards

1
Q

why do we need proteins in our diet?

A

for growth and repair

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2
Q

foods that are rich in protein

A

meat, fish, lentils, tofu, chickpeas

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3
Q

what are proteins?

A

large, important molecules (polymers) found in our bodies
each protein within the body has a specific function that is related to its shape.
they are condensation polymers made up of many amino acid molecules linked together

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4
Q

2 types of protein shape

A
  1. fibrous (fibres, long chains)

2. globular (globule, spherical shape)

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5
Q

Fibrous proteins

A

long and thin and are the major structural materials of animal tissue

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6
Q

globular proteins

A

spiral chains folded into compact units.

involved in the maintenance and regulation of life processes and include enzymes and many hormones.

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7
Q

Collagen

A

found in tendon, muscle, bone
functions - structural support
nature - fibrous

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8
Q

Keratin

A

found in hair, skin and nails
function - structural support
nature - fibrous

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9
Q

Insulin

A

found in pancreas
function - hormone to help control blood glucose levels
nature- globular

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10
Q

what are proteins made up of?

A

amino acid molecules joined together

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11
Q

what are amino acids?

A

the building blocks from which proteins are formed

they contain an amino (amine) group (-NH2) and a carboxyl group (-COOH) attached to the same carbon (alpha carbon)

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12
Q

Structure of proteins: what is R?

A

a variable organic group or a hydrogen

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13
Q

Structure of proteins: Phenylalanine

A

amine and carboxyl groups attached to carbon

R= CH2 and benzene ring

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14
Q

what are essential amino acids?

A

the amino acids that cannot be made in our body.

they must be present in our diet.

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15
Q

condensation polymerisation

A

condensation: molecules join together and water is eliminated.
polymerisation: single units (monomers) joining together to form a large chain of many units (polymer)

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16
Q

condensation reaction

A

the amino group on one amino acid and the carboxyl group on a neighbouring amino acid join together, with the elimination of water

17
Q

what is the link that forms between two amino acids called?

A

an amide link (-CONH)

also known as peptide link

18
Q

what is a tripeptide

A

polymers made up of only 3 amino acids

19
Q

what is a polypeptide

A

polymer made up of a large number of amino acids

20
Q

structural formula of condensation polymerisation

A

-OH removed from carboxyl group and -H removed from amine group.

21
Q

when are proteins broken up?

A

during digestion process called hydrolysis to produce amino acids

22
Q

breakdown of proteins

A

a water molecule causes the splitting

N-C bond is broken

23
Q

steps for hydrolysis of proteins

A
  1. identify the amide links
  2. break apart C-N bonds
  3. redraw individual structures
  4. add -OH to make carboxyl groups and -H to complete amine group
24
Q

general condensation definition

A

when molecules join together with the elimination of a small, stable molecule (eg water)

25
Q

general hydrolysis definition

A

when large molecules are broken down into smaller molecules by reaction with water

26
Q

what is chromatography?

A

a technique that allows us to separate substances in a complex mixture

27
Q

describe paper chromatography

A

HP- hydrolysed protein (mixture of different proteins)
A-D pure samples of various amino acids

solvent added- mobile phase
the extent to which molecules travel up paper depends on size/polarity

no of spots=no of amino acids present
if spots on HP same height as amino acid A-D they are the same

28
Q

what can be done if the hydrolysed protein contains an amino acid that does not match

A

another chromatogram can be run with different known samples of pure amino acids.

29
Q

what are enzymes

A

proteins which act as biological catalysts

30
Q

Enzymes are specific for particular chemical reactions. Give an example

A

Pepsin only catalyses the hydrolysis of proteins and not any other chemical reaction

31
Q

what is the active site

A

certain sequences of amino acids form a region known as the active site
the shape of the active site allows specific reactants, known as substrates, to attach (like lock and key)

32
Q

what happens to incorrect substrates

A

they are unable to fit the shape of the active site and are not changed

33
Q

what is enzyme function related to

A

molecular shapes of proteins

34
Q

process of catalysis by enzymes

A
  1. substrate approaches active site
  2. substrate attaches to active site
  3. substrate becomes products
  4. products released and active site free to react again
35
Q

how do protein chains react with themselves

A

intermolecular bonding (often hydrogen bonding)

36
Q

intermolecular bonding in proteins

A
  • gives the protein a particular shape and creates an ‘active site’ which is unique to that enzyme
  • only specific, complementary substrates will fit into this active site
37
Q

denaturing enzymes

A

-when the temperature is increased too much or the acidity increases too high the intermolecular bonds will break.
-this means the protein chain will unravel, destroying the active site
-the substrate can no longer bind and so the enzyme no longer functions as a catalyst
(graph of enzyme activity vs temp/pH with narrow optimum range)

38
Q

a real-life example of denaturing proteins

A

the protein albumin in eggs becomes denatured and changes colour and texture