Proteins Flashcards

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1
Q

What are proteins?

A

Polymers made of monomers called amino acids

The sequence, type & number of amino acids within a protein determines its shape & function

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2
Q

What are the structure of Amino acid?

A

General structure: a central carbon atom, an amine group (-NH2), a carboxylic acid group (-COOH), a hydrogen atom & an R group (differs depending on the amino acid)

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3
Q

What is a peptide bond?

A

Peptide bonds form between an amine group of one amino acid and a carboxylic acid group of another → water is released (a condensation reaction)

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4
Q

What is dipeptides?

A

Are formed by the condensation of two amino acids

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5
Q

What is oligopeptides?

A

Are formed by the condensation of ~3 amino acids

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6
Q

What is polypeptides

A

Are formed by the condensation of 3+ amino acids

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7
Q

Protein structure

A

A functional protein may contain one or more polypeptides.

There are four levels of structure in proteins

Different chemical bonds in each level allow proteins to have different structure & functions:

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8
Q

What bonds increase in strength?

A

Hydrogen bonds - between polar R groups

Weak hydrophobic interactions - between nonpolar R groups

Ionic bonds - between +ve & -ve charged R groups (can be broken by pH changes)

Disulphide bonds / bridges - a covalent bond between cysteine R groups

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9
Q

Primary structure of a protein

A

Primary structure: the sequence of amino acids bonded by covalent peptide bonds

Specific for each protein

DNA determines the primary structure through protein synthesis → affects the shape → affects the function

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10
Q

Secondary structure of a protein

A

Secondary structure: hydrogen* bonding between amino acids enable two shapes to form:
Α-helix - H bonds between every 4th peptide bond
β-pleated sheet - H bonds between parallel parts of a polypeptide chain

Most fibrous proteins have a secondary structure

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11
Q

Tertiary structure of a protein

A

Tertiary structure: more conformational changes & additional bonds form between R-groups

-Hydrogen bonds
-Disulphide
-Ionic
-Weak hydrophobic interactions

This structure is common in globular proteins

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12
Q

Quaternary structure of a protein

A

Quaternary structure: Occurs in proteins that have more than one polypeptide chain working together as a functional macromolecule

Each polypeptide chain is called a subunit of the protein

A good example is haemoglobin

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13
Q

Biochemical test for proteins

A

Biuret solution
Positive= purple
Negative = Blue

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14
Q

Example of a globular protein: Haemoglobin

A

Quaternary structure (4 polypeptide chains)

4 subunits (two α–globins and two β–globins) held together by disulphide bonds

Each subunit contains a haem prosthetic group: these contains Fe2+ which reversibly combine with oxygen molecules → forms oxyhaemoglobin (+ what makes blood red!)

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15
Q

Example of a fibrous protein: Collagen

A

Three polypeptide chains held together by H bonds → form a triple helix - tropocollagen

Each polypeptide chain is a helix shape & contains lots of glycine, proline & hydroxyproline amino acid monomers

Covalent cross links also form between multiple triple helices → form collagen fibrils

Many fibrils are then arranged together to form collagen fibres

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