Proteins Flashcards

(22 cards)

1
Q

What are the monomer that make up polypeptides?

A

Amino acids

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2
Q

What do polypeptides combine to form?

A

Proteins

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3
Q

What are the four chemical groups attached to the central carbon atom in an amino acid?

A
  1. Amino group (NH3)
  2. Carboxyl group (COOH)
  3. Hydrogen atom (H)
  4. R (side) group
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4
Q

What determines the differences between the 20 naturally occurring amino acids?

A

The R (side) group, which varies between each amino acid

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5
Q

What type of reaction forms a peptide bond between two amino acids?
Outline the full process of forming a peptide bond
> What is removed during the formation of a peptide bond
> What groups combine to form a peptide bond?

A

A condensation reaction occurs between two amino acids to form a dipeptide. The -OH from the carboxyl group of one amino acid and the -H from the amino group of another come together form the peptide bond, with the removal of a water molecule.

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6
Q

What is a dipeptide?

A

A molecule formed when two amino acids join together by a peptide bond

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7
Q

How can a peptide bond be broken?

A

By hydrolysis, which involves the addition of a water molecule

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8
Q

What is polymerisation in the context of proteins?

A

The process in which many amino acid monomers join together through condensation reactions to form a polypeptide

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9
Q

What is the primary structure of a protein, and what determines the primary structure?

A

The specific sequence of amino acids in a polypeptide chain, which is determined by the DNA

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10
Q

How does the primary structure of a protein determine its function?

A

The sequence of amino acids dictates the protein’s shape, which is essential for its specific function

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11
Q

What happens if a single amino acid in the primary structure is changed?

A

It may alter the protein’s shape, affecting or preventing it’s ability to function

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12
Q

What is the secondary structure of a protein, and what is the main bond responsible for the secondary structure of proteins?

A

This is the structure that forms when weak hydrogen bonds form between the primary structures, causing the chain to twist into a 3D shape (like a helixes or beta pleated sheets)

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13
Q

What is the main difference between a a-helix and a B pleated sheet?

A

An a - helix is a coiled structure, while a B pleated sheet consists of polypeptide chains lying parallel or antiparallel in a folded, sheet - like arrangement

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14
Q

What is the tertiary structure of a protein?

A

The tertiary structure occurs when there is even further twisting and folding of the secondary structure into a complex specific 3D shape

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15
Q

Why is the tertiary structure important for protein function?

A

It determines the protein’s shape, allowing it to recognise and interact with other molecules in a specific way

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16
Q

What are three types of bonds that maintain the tertiary structure of a protein?

A

Disulfide bridges
Ionic bonds
Hydrogen bonds

17
Q

What are disulfide bridges?

A

Strong covalent bonds which are not easily broken

18
Q

What are hydrogen bonds in the tertiary structure?

A

They are numerous but weak, easily broken by temperature or pH chaneges

19
Q

How does the primary structure of a protein influence its tertiary structure?

A

The sequence of amino acids determine where bonds form, shaping the final 3D structure

20
Q

What is the quaternary structure of a protein?

A

A structure where multiple polypeptide chains are linked together, sometimes with non - protein groups

21
Q

How do polypeptide chains interact in the quaternary structure?

A

They are linked in various ways to form a larger, function protein

22
Q

What is an example of protein with a quaternary structure?