Proteins Flashcards

(36 cards)

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
Lock and Key
Substrate is completly complementary in shape to the enzymes active site Perfect fit No change in shape
26
Induced Fit
Substrate and Active site are complementary but not completly Not an exact match Slight change in shape
27
pH of a solution
Measure of its hydrogen ion concentration
28
Calculating pH
pH = -log10[H+] [H+] = 10^-pH
29
Measure enzyme activity
Formation of products or disappearance of substrate
30
Enzyme-Substate Complexes
Enzyme-Substate Complexes
31
Rate
change / time change in y / change in x
32
For a reaction to occur
Must be contacts between sunstarte and active site of enzyme
33
Increase Contact
increase temperature increase concentration of substrate increase concentration of enzyme
34
Competative Inhibitor
Different molecule with the same shape binds to active site instead of substare stops formation of enzyme-substate complexes
35
Non Competative Inhibitor
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
Enzyme Activation
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