Chapter 3 Proteins Flashcards

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1
Q

What is the general structure of an amino acid?

A

COOH—R—NH2

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2
Q

What part of proteins determine function?

A

The R groups of amino acids, which result into precise shapes

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3
Q

What bonds amino acids together? What is formed and how is it reverse

A

Condensation to bond
Dipeptide to Polypeptide
Hydrolysis

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4
Q

What is the primary structure of proteins?

A

The sequence of the amino acids

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5
Q

What is the secondary structure of proteins?

A

When the chain of amino acids coils to form an alpha helix or beta pleated sheet, formed from hydrogen bonds between N & H and O & H.
If it is between every 4 amino acids = helix
If it is between every 6 amino acids= sheet

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6
Q

What is the tertiary structure of proteins and how is it formed?

A

The folding of a secondary structure, to form a very precise 3D shape
It is formed due to interactions between R groups of amino acids which stick out

Interactions include:
Ionic Bonding
Hydrogen Bonding
Disulphide bridges
London Forces / Permanent dipole-dipole

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7
Q

What are the uncoiled polypeptide chains called in a protein?

A

Amorphous regions

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8
Q

What is the quaternary structure of proteins?

A

The association of two or more amino acid subunits/ polypeptide folded chain, due to London Forces/ Permanent Dipole…, Hydrophobic/ Hydrophilic interactions, Ionic Bonds, Hydrogen Bonds, Disulphide bridges

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9
Q

What test is used to test for proteins?

A

Bierets
Pale blue to purple

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10
Q

What is globular protein and describe how it formed?

A

Spherical shaped, soluble proteins
Protein folds in tertiary so the hydrophobic R groups are pointed inwards, kept away from the aqueous environment
Hydrophilic R groups on outside

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11
Q

What is a simple protein? What is a conjugated protein?

A

Conjugated- globular protein containing a non-protein inorganic component called a prosthetic group
Simple Proteins- ones without a prosthetic group

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12
Q

Describe the structure of haemoglobin and how it related to its function

A

Haemoglobin in a globular, quartenary protein with 2 alpha and 2 beta subunits. It is a conjugated protein contains four haem groups, which bind reversibly to oxygen
It is water soluble which is necessary when it is find in high concentrations in the cytoplasm
Can change shape

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13
Q

Describe the structure of a name enzyme and function

A

Catalase is a quartenary protein with 4 haem groups. It’s function is to catalyse and speed up the break down of H2O2 a toxic product of metabolism , when it builds up

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14
Q

What is a fibrous protein?

A

Long insoluble proteins which contain a high proportion of hydrophobic R groups. They are unreactive and very strong, and flexible. They normally have a repetitive base structure and then to make strong, long, unfolded proteins. They play a structural role such as protective with keratin and nails, or to give elasticity like elastin

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15
Q

What is the function of Keratin?

A

Protective role
Used to help form tissues of nails, hair and outer layers of skin
Lots of disulphide bridges (with the number of these bonds determining flexibility). Lots of amino acid cysteine

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16
Q

What is the function of elastin? Give an example

A

Quartenary protein made from many stretchy molecules called tropoelastin. Found in elastic fibres with other protein fibres. Gives flexibility when needed. E.g in Blood Vessels, and alveoli, so they can expand and return to normal size

17
Q

What is the structure and function of collagen?

A

Used in connective tissues and blood vessels
3 polypeptides wound in a long and string rope structure