3.6 Structure Of Proteins Flashcards

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1
Q

What do all amino acids have in common and what distinguishes them from each other

A

Amine group (NH2)
R group distinguishes
Carboxyl cooh group

NH2C(R group)(H)COOH

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2
Q

How do the synthesis of proteins happen ?

  • what enzyme does it?
A

Peptide bond - H2O is lost and C of carboxyl group and N of amine group will form a covalent bond . Thus condensation reaction , CONH

2) then multiple Amino acids join by peptide bonds , catalysed by enzyme peptidyl transferase present in ribosomes to make polypeptide

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3
Q

What is primary structure of a protein?

What is it determined by ?

A

The primary structure describes the linear sequence of the amino acids in the polypeptide

  • determined by DNA( as it has sequence transported by mRNA and determines order etc)
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4
Q

What is secondary structure of a protein?

What is it determined by ?

What do they make ?

A
  • Here the first folding of a protein takes place
  • due to HYDROGEN bonds between the O on carboxyl acid and And H bonded to N on amino groups
  • type of folding determined by the ORDER OF AMINO ACIDS , as then hydrogen bonds either make alpha helix or beta pleated sheet
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5
Q

What is tertiary structure ?

What is it determined by ?

Why- why determined by and what does this make?

A

The FURTHER FOLDING of a protein to make final shape

  • determined by interactions of R GROUPS
  • also determined by secondary structure

: because alpha helix will become GLOBULAR PROTEINS
: beta pleated sheets will become a FIBROUS PROTEINS

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6
Q

What types of R groups interactions are there for tertiary structure ?

A

1) Hydrogen bonding
2) Hydrophilic and hydrophobic interactions = Weak van def waal forces
3) disulphides bridge - covalent bond between two Sulphur atoms (from cysteine )
4) Ionic bonds - between negatively and positively charged R groups

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7
Q

Quaternary structure ?

A

: reactions between different polypeptide chains known as subunits
- can be the same interactions as tertiary but difference is they between whole subunits now

For example haemoglobin contains 4 chains with two sets of identical units , this is the quaternary structure …

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8
Q

How to test for proteins again quick

A

Biurets test- blue solution based of a copper sulfate ALKALINE solution )

  • add it, if it goes purple , then it is positive
  • here in the presence of a peptide bond, Cu (II) ions will become reduced to form a violet lilac complex in an alkaline solution

Alternatively mix sample with equal volum of 10% NAoH and 1% copper sulfate , so that it is alkaline then do it normally etc

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9
Q

What are some basic functions of proteins ?

A
  • enzymes
  • for signalling (glycoproteins act as receptors , but also peptide hormones )
  • structural (keratin in hair, collagen between bones)
  • contractile (spindle fibres, muscles actin )
  • storage (white of an egg as albumin)
  • transport (haemoglobin oxygen)
  • defensive (antibodies )
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10
Q

How does a protein split again?

A

Protease enzyme and hydrolysis reaction, here add water and peptide bond breaks to reverse to amino acids

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11
Q

Amino acid most common snd what can they be

A

They can be ph buffers and the most common is glycine

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