Proteins Flashcards

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1
Q

Subunits

A

Amino Acids

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2
Q

Amino Acids general structure

A

Amino group, variable side chain, carboxyl group

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3
Q

How many different amino acids are there

A

@0

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4
Q

What elemnts do Amnio Acids contain

A
Carbon 
Hydrogen 
Oxygen 
Nitrogen 
and sometimes Sulfur
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5
Q

2 amino acids make a

A

dipeptide

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6
Q

Bond in a dipeptide

A

peptide bond

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7
Q

Structures of a protein

A

Primary
Secondary
Tertiary
Quaternary

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8
Q

Primary structure

A

Sequence of amino acids in the polypeptide chain

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9
Q

Primary structure bonds

A

Peptide bonds

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10
Q

Secondary structure

A

Initial folding of a polypeptide chain

Alpha helix and Beta pleated sheets

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11
Q

Secondray structure bonds

A

Hydrogen bonds

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12
Q

Tertiary structure

A

Further folding to give the fianl 3D form

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13
Q

Tertiary structure bonds

A

Hydrogen bonds
Disulphide bonds
Ionic bonds
Hydrophobi/hydrophilic interactions

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14
Q

Quaternary structure

A

Many polypeptide chains in tertiary structure together

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15
Q

Prostectic group

A

Some proteins have non proteins groups attached

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16
Q

Fibrous proteins

A

Long fibres/sheets
Insoluble in proteins
Structural role

17
Q

Globular proteins

A

Spherical/globe like
Soluble in water
Biomedical functions (enzymes)
metabolic function

18
Q

Denaturation

A

Permanent change in shape

19
Q

Temperature

A

weak bonds are broken

alters tertiary structure so unable to carry out function

20
Q

pH

A

disrupt hydrogen and ionic bonds
alters tertairy structure
unable to cary out functions

21
Q

Enzymers Are Proteins

A

Enzymers Are Proteins

22
Q

Enzymes

A

Biologicalcatalysts

increase rate of reaction

23
Q

Activation Energy

A

minimum amount of energy required for a reaction to occur

24
Q

How do enzymes affect Activation Energy

A

enzymes lower the activation energy

allows reactions to take place in the body

25
Q

Lock and Key

A

Substrate is completly complementary in shape to the enzymes active site
Perfect fit
No change in shape

26
Q

Induced Fit

A

Substrate and Active site are complementary but not completly
Not an exact match
Slight change in shape

27
Q

pH of a solution

A

Measure of its hydrogen ion concentration

28
Q

Calculating pH

A

pH = -log10[H+]

[H+] = 10^-pH

29
Q

Measure enzyme activity

A

Formation of products
or
disappearance of substrate

30
Q

Enzyme-Substate Complexes

A

Enzyme-Substate Complexes

31
Q

Rate

A

change / time

change in y / change in x

32
Q

For a reaction to occur

A

Must be contacts between sunstarte and active site of enzyme

33
Q

Increase Contact

A

increase temperature
increase concentration of substrate
increase concentration of enzyme

34
Q

Competative Inhibitor

A

Different molecule with the same shape
binds to active site instead of substare
stops formation of enzyme-substate complexes

35
Q

Non Competative Inhibitor

A

Molecule binds to enzyme at the allosteric site
changes active site shape
substrate can no longer fir and bind
stops formation of enzyme-substrate complexes

36
Q

Enzyme Activation

A

molecule can bind as an inhitior but instead of stopping the formation of enzyme-substrae complexes
it allows binding and actiavtes the enzyme for enzyme-substare completes to form