Proteins Flashcards

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1
Q

What are 4 roles of amino acids and give an example for each?

A

Structure: muscle

Catalytic: enzymes

Cell signalling: hormones

Immunological: antibodies

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2
Q

What is the general structure of an amino acid?

A

On the left is the amino group: 2 separate hydrogen atoms are single bonded to a nitrogen atom

On the bottom is the R group which is represented by R

On the right is the carboxylic acid group: an OH is single bonded to a carbon and an Oxygen is double bonded to the same carbon

In the middle is a Carbon that the nitrogen and carbon from the other groups bind to and above it is a hydrogen atom

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3
Q

How do amino acids form and break?

A

Form: During a condensation reaction 2 amino acids will be joined to together by a peptide covalent bond and form a dipeptide molecule

Break: During a hydrolysis reaction the peptide covalent bond is broken and water is added which causes two amino acids to be formed

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4
Q

How many naturally occurring amino acids are there?

A

20

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5
Q

What are polypeptides and how are they formed?

A

They are long chains of amino acids which are formed as more amino acids are added to dipeptides through condensation reactions that release water and form peptide bonds

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6
Q

What is the primary structure of a protein?

A

The order of amino acids that is held together by peptide bonds

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7
Q

What is the secondary structure of proteins?

A

The areas of initial folding. The structure is held together by hydrogen bonds in main structures called alpha helix and beta pleated sheets

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8
Q

What is the tertiary structure of proteins?

A

Interactions of the R groups, it is given a 3D shape as it is held together by 4 bonds and interactions: hydrogen bond, disulphide bridge, ionic bond and a cluster of hydrophobic groups behind the hydrogen bond

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9
Q

How are hydrogen bonds formed and how strong are they?

A

Slightly +charged H and slightly-charged O come into close contact it forms hydrogen bonds.

They are very weak

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10
Q

How are ionic bonds formed and how strong are they?

A

Ionic bonds are formed when oppositely charged R groups come into close contact with one another.

They aren’t particularly strong

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11
Q

How are disulphide bonds/bridges formed?

A

A disulphide bond is formed between cysteine molecules which contain sulfur. When the cysteines are close they form double covalent bonds.

They are very strong and heard to break

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12
Q

Where do hydrophobic and hydrophilic interactions take place?

A

In a water based environment hydrophobic amino acids will be most stable when there is no water present.

The hydrophilic amino acids will be found on the outside and hydrophobic in the inside

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13
Q

What is the quaternary structure of a protein?

A

The product of two or more polypeptides joining together or if a prosthetic group is present.

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14
Q

How does denaturing occur and what does it do?

A

Denaturing occurs when the bonds of a protein are broken

It mostly happens in hydrogen and ionic bonds as they are the weakest

It can be caused by changes in temperature, pH or salt concentration

Fibrous proteins lose their structural strength when denatured whereas globular proteins become insoluble and inactive

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15
Q

What are globular proteins and what is their structure like?

A

Spherical proteins that are caused by tightly folded polypeptide chains

The chains are usually folded so that hydrophobic groups are on the inside and hydrophilic groups on the outside which makes most globular proteins soluble in water

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16
Q

What are the roles of globular proteins and give an example for each?

A

Transport proteins such as haemoglobin

Enzymes such as amylase

Hormones such as insulin

17
Q

Haemoglobin is a globular protein, describe its structure

A

Made of 4 polypeptide chain subunits: 2 alpha, 2 beta

within 4 subunits there are 4 prosthetic groups which each contain Fe2+

It’s a conjugated protein as it is a globular protein with a prosthetic group

It is soluble

18
Q

Amylase is an enzyme made from a globular protein, describe its structure and its function

A

It is soluble

It is made from a single chain of amino acids

Its secondary structure has alpha helices and beta pleated sheets

It only works if the co-factor Cl- is bound to it

Its function is to break down starch into maltose

19
Q

Insulin is a hormone made from a globular proteins, describe its structure and its function

A

It is soluble

It is made of 2 amino acid chains that are joined together by disulphide bonds

Its function is to turn glucose into glycogen and store it in muscle tissue and the liver

20
Q

What are the functions of Fibrous proteins?

A

They make up keratin and elastin

21
Q

What is the structure of fibrous proteins like?

A

Formed from parallel polypeptide chains that are held together by cross-links

They form long, rope-like fibres, with high tensile strength

Generally insoluble in water

22
Q

What is the use of keratin? Give 3 examples

A

Provides protection on animals

Hair, claws, feathers, hooves, nails

23
Q

What is the function of elastin? Give 3 examples

A

Major component in tissues that require elasticity

Arteries, lungs, bladder, skin, cartilage

24
Q

What are 3 characteristics of fibrous proteins?

A

Insoluble
Elongated
Forms cross-links
High tensile strength
Flexible

25
Q

What are 4 characteristics of globular proteins?

A

Soluble
Spherical
3D shape
Complementary to another molecule
Sensitive to pH and temperature
Can contain a prosthetic group
Hydrophilic on the outside