3.1.4 Proteins Flashcards

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1
Q

What are proteins made out of?

A

Amino acids

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2
Q

What is a dipeptide

A

2 amino acids

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3
Q

What’s a polypeptide?

A

More than 2 amino acids

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4
Q

What is a protein ?

A

One or more polypeptides

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5
Q

What elements make up proteins?

A

C, H, O, N
Some have S

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6
Q

Draw and amino acid

A

H H O
\ | //
H - N-C-C
/ | \
H R O

COO is carboxyl
R=R-group (variant)
NH3 = amino

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7
Q

How many R groups are there?
And how many amino acids?

A

20 R groups
20 amino acids

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8
Q

Peptide bonds are formed between which groups?
What type of reaction?

A

Amino and carboxyl
Condensation

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9
Q

Which elements hold the peptide bond?

A

Nitrogen and carbon

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10
Q

Describe the first level of protein structure

A

Primary structure

Order of amino acids in a polypeptide

Determines shape and function of protein

A change in 1 amino acid can change the shape and may stop its function

Linked by only peptide bonds

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11
Q

Describe the 2nd level of protein structure

A

Chains fold into 2 different shapes:
Alpha helices(most common)
Beta pleated sheets(less common)

Hydrogen bonds between CO and NG of adjacent amino acids (no r groups involved )

Found in all proteins

R groups are stuck out to the side ready for bonding in the tertiary structure

Secondary structure

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12
Q

Describe the 3rd level In protein structure

A

Further folding caused the R group bonding and forms a 3D shape

Contains hydrogen bonds(weak) ionic bonds (stronger but vulnerable to changes in PH) Disulphide bridge(very strong covalent bonds)

This makes a globular protein(3D)

Has hydrophobic interactions

Tertiary structure

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13
Q

What is a disulphide bond?

A

2 sulfur atoms bonded (split by reducing agents)

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14
Q

What is the 4th level of protein structure?

A

Quaternary structure

2 or more polypeptide chains combine

Joined by bonds same as tertiary (H, disulphide bonds, ionic)

Only some proteins exhibit quaternary structure

Example: haemoglobin consists of 4 polypeptide chains held by disulphide bonds bridges and non protein prosthetic group

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15
Q

Protein shape to function

A

Roles depends upon their molecular shape-2 types:
Fibrous- proteins like collagen have structural roles - polypeptide chains linked in parallel chains or sheets with numerous cross linked to make fibres

Globular- perform metabolic functions- shape is compact and folded spherical

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16
Q

Fibrous - globule similarities and differences

A

Fibrous:
Structural function
Regular repetitive sequences
H bonding
Cross linked to form long fibres
Stable
Insoluble in water

Globular:
Metabolic function
Irregular sequences (spherical shape)
H, ionic and disulphide bridges/bonding-hydrophobic bonds
Depressions(other molecules can fit in)
Relatively unstable
Soluble in water

17
Q

Function of proteins

A

Transport
Movement
Sensitivity and coordination (nervous system and hormone system)
Reproduction
Protection(immune system)

18
Q

Method to test for proteins

A

Place sample of solution in test tube and add equal volume of biurets reagent

If present then solution is purple/lilac

Of negative results solution stays blue