Proteins

0.0(0)
Studied by 0 people
call kaiCall Kai
learnLearn
examPractice Test
spaced repetitionSpaced Repetition
heart puzzleMatch
flashcardsFlashcards
GameKnowt Play
Card Sorting

1/39

encourage image

There's no tags or description

Looks like no tags are added yet.

40 Terms

1
New cards

Give the general structure of an amino acid and what each respresents

NH2 - Amine

COOH- Carboxyl

R - Side chain

<p>NH<sub>2</sub> - Amine</p><p>COOH- Carboxyl</p><p>R - Side chain </p>
2
New cards

What are proteins?

They are polymers made up of amino acid monomers

3
New cards

How many amino acids are common in all organisms and how do they differ?

  • 20 amino acids

  • They differ only in their side group


4
New cards

What is a peptide bond?

A bond formed between 2 amino acids through a condensation reaction, where water is removed

5
New cards

How are dipeptides formed?

  • A condensation reaction between 2 amino acids


6
New cards

How are polypeptides formed?

Through the condensation of three or more amino acids

7
New cards

How many polypeptides are needed for a functional protein?

One or more polypeptides

8
New cards

Draw a peptide bond

knowt flashcard image
9
New cards

What happens during hydrolysis of a protein? (3)

  • Addition of water

  • Breaks the peptide bonds

  • Resulting in polypeptides being broken down into amino acids


10
New cards

Which levels of protein structure relate to a single polypeptide chain?

The primary, secondary and tertiary stages

11
New cards

Describe the primary structure of all proteins and what is the name given to this structure?

  • It is a sequence of amino acids linked together by peptide bonds through condensation reactions

  • (always mention these when asked about primary structure in any form)

  • A polypeptide.


12
New cards

How is the primary structure of a protein determined?

It is determined by DNA. 

  • By instructing the cell to add certain amino acids in specific quantities in a certain sequence, during translation.

  • This affects the shape and, therefore, the function of the protein


13
New cards

Describe the secondary structure of a protein

The local coiling or folding of the polypeptide chain occurring as a result of the hydrogen bonding between amino acids in the peptide backbone which does not involve r groups


14
New cards

What bonding is the secondary structure of a protein held by, which groups form this bond and what are the charges?

  • Hydrogen bonding.

  • This hydrogen bond forms between the H in the -NH- region and the oxygen in  the -C=O region of another amino acid

  • The hydrogen in the -NH- region has a partially positive charge while the oxygen in the -C=O- group has a partially negative charge


15
New cards

Which 2 factors can easily break this secondary structure and why?

  • High Temperature and high pH

  • This is because of the hydrogen bonds which hold the secondary structure together which are easily broken by high heat and pH changes


16
New cards

Which 2 types of shape can be formed due to these hydrogen bonds?

  • α-helix

  • β-pleated sheet


17
New cards

When does the alpha helix shape occur?

The α-helix shape occurs when the hydrogen bonds form between every fourth peptide bond.

<p><span><span>The </span></span><strong>α-helix</strong><span><span> shape occurs when the hydrogen bonds form between every </span></span><strong>fourth</strong><span><span> peptide bond. </span></span></p>
18
New cards

When does the beta sheet shape occur?

  • The β-pleated sheet shape forms when the protein folds so that two parts of the polypeptide chain are parallel to each other

  • This enables hydrogen bonds to form between the folded layers


<ul><li><p>The <strong>β-pleated sheet </strong>shape forms when the protein folds so that <strong>two parts of the polypeptide chain</strong> are <strong>parallel</strong> to each other</p></li><li><p>This enables hydrogen bonds to form between the folded layers</p></li></ul><p></p>
19
New cards

For which type of proteins is the secondary structure the highest folding level for?

  • Fibrous proteins


20
New cards

What is the tertiary structure of a protein?

  • Unique 3D structure where bonds which form between the side chains (r-group) of the protein due to the twisting and folding of the secondary structure.


21
New cards

What are the 4 types of additional bonds which can form in the tertiary structure of proteins?

  • Hydrogen bonds

  • Disulfide bridges

  • Ionic bonds

  • Hydrophobic interactions


22
New cards

List the the additional bonds in order of strongest to weakest

Disulfide bonds

Ionic Bonds

Hydrogen bonds

Hydrophobic interactions

23
New cards

Features of disulfide bonds (3)

  • Forms between 2 cysteine R groups and helps to stabilise proteins

  • Broken by reduction

  • Common in proteins secreted from cells (eg insulin)


24
New cards

Features of ionic bonds (3)

  • Forms between positively charged amine group and negatively charged COO- groups

  • Stronger than hydrogen bonds but not common

  • Broken by pH changes


25
New cards

Features of hydrogen bonding(2)

  • Forms between strongly polar r groups

  • Weakest bonds that form


26
New cards

Define quaternary structure of a protein

When there is more than 1 polypeptide chain working together as a functional macromolecule


27
New cards

List 6 functions of protein (THEACS)

  • Enzymes: biological catalysts to speed up metabolic reactions

  • Transport proteins (eg. Channel and carrier proteins/haemoglobin)

  • Structural proteins: provide support (collagen in connective tissue, keratin in hair and nails)

  • Hormones: Regulate processes (eg insulin)

  • Antibodies: Part of the immune response

  • Contractile proteins: Enable movement (actin and myosin in muscle)


28
New cards

Biochemical test for protein

  • Biuret reagent


29
New cards

Colour change for biochemical test for protein

Blue to purple


30
New cards

What must be present for the biochemical test to work?


There must be at least 2 peptide bonds present

  • There will be a negative result if there is only amino acids or dipeptides


31
New cards

What are prosthetic groups?

Non-protein structure that is permanently integrated into an enzyme or protein's structure

32
New cards

What is an example of a prosthetic group?

Heme


33
New cards

What are conjugated proteins?

A complex protein consisting of a simple amino acid shell bound to a non-protein chemical component.

34
New cards

What are examples of conjugate proteins? (3)

  • Glycoproteins

  • Lipoproteins

  • Haemoglobin


35
New cards

What is a globular protein?

A protein that folds into a compact, roughly spherical 3D shape, which is soluble in water

36
New cards

What are features of a globular protein? (3)

  • Compact and spherical (describes the 3D tertiary structure).

  • Hydrophilic R-groups on the outside (to form hydrogen bonds with water).

  • Globular proteins carry out functional or metabolic roles due to highly specific shapes


37
New cards

Examples of globular proteins

  • Haemoglobin

  • Enzymes

  • Antibodies


38
New cards

What are fibrous proteins?

Proteins which are in long, parallel strands and insoluble in water

39
New cards

What are features of a fibrous protein? (3)

  • No tertiary folding

  • Insoluble in Water: Because hydrophobic R-groups face outwards, they are completely insoluble.

  • Structural Role: They provide mechanical strength, elasticity, and protection to structural tissues.


40
New cards

Examples of fibrous proteins and where they are found(3)

  • Collagen: Found in tendons, bones, cartilage, and walls of blood vessels.

  • Keratin: Found in hair, nails, and the outer layer of skin.

  • Elastin: Found in elastic connective tissue (like the lungs, large arteries like the aorta, and skin