Bio Mols Proteins Flashcards

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1
Q

What 4 elements do proteins contain

A
Carbon 
Hydrogen 
Oxygen 
Nitrogen 
Sometimes sulphur
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2
Q

What is the monomer sun Inuit of proteins

A

Amino acids

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3
Q

How many proteins are commonly occurring in all living organisms

A

20

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4
Q

What two groups do amino acids always have?

What group differs in amino acids?

A

Amino agouti NH2
Carboxylic acid group COOH

Differ in the atomic group R

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5
Q

Amino acids are joined by what reaction?
What bond?
What’s the formulae of the bond

A

Condensation

Peptide bond COHN

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6
Q

Two amino acids join to form a

A

Dipeptide

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7
Q

Many amino acids join together in a chain to form

A

Polypeptide

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8
Q

What does a protein consist of

A

One or more polypeptides

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9
Q

What is the general structure of an amino acids

A

H. R. Double bond O

      N.        C.            C 

H H OH

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10
Q

What is the amino acids formulae

A

NH2

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11
Q

What is the carboxylic acid formula

A

COOH

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12
Q

How can proteins be hydrolysed

A

Heating with acid

Using the enzyme proteases at the optimum temp

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13
Q

How do proteins vary 3

A

Number and type and sequence of amino acid

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14
Q

How are proteins classified

A

Occurring to their structure

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15
Q

What is the primary structure of a protein 3

A

Sequence of amino acids
Joined by peptide bond
On polypeptide chain

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16
Q

What does the sequence of amino acids determine

A

The specific shape of the protein

17
Q
What does the secondary structure refer to? 
Why? 
What bonds form? 
Between where?
5 
What structures?
A

The folding or
Coiling
Of the polypeptide chain as a result of hydrogen bonding between the amino acids

Alpha helix or beta pleated sheet

18
Q

What is the tertiary structure

What does this determine in enzymes

A

Further coiling and folding of secondary structure due to
Hydrogen Ionic and Disulfude bridges

Determines the shape of the active site and its precise function in enzymes

19
Q

What two types of tertiary proteins are thee

A

Globular

Fibrous

20
Q

What is a globular protein?
Example 2
Are they soluble
Do they have a specific structure

( from alpha helix)

A

Highly folded and coiled polypeptide chain to produce compact and complex tertiary structure.
Eg enzymes and antibodies
Soluble and have specific structure

21
Q

What is a fibrous protein structure
Are they soluble
What is their function
Eg

(From beta pleated sheet)

A

Long and thin and insoluble
Structural functions
Eg keratin in hair
Collagen in tissue

22
Q

What do quaternary structure relate to?

Which bonds?

Eg

A

Complex protein consisting of more than one polypeptide chain

Ionic bonds, hydrogen bonds, disulfide bridges and hydrophobic interactions

Proteins will behave similarly to phospholipids in water; the polar groups will form favorable interactions on the surface with water, while the hydrophobic groups will be in the core and away from the water molecules. Usually, amino acids with non-polar residues will be found in the core of proteins.

23
Q

What is denaturation of proteins

A

Altercation in the tertiary structure of a protein

Often irreversible of the 3D shape and is no longer functional

24
Q

What is denaturation usually caused by?
What can cause this? 3
Which bonds are not broken at the temperature?

A

Breaking hydrogen and ionic bonds
Disulfide bonds

High temperature
Extreme change in pH
Heavy metals

25
Q

What is the test for protein

A

Biuret test

26
Q

Explain the biuret test

A

Add Biuret reagent
= purple present
Remains blue not present