Proteins Flashcards

(34 cards)

1
Q

How many naturally occurring amino acids are there

A

20

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2
Q

Draw an amino acid

A

Draw on white board and check note

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3
Q

What do all amino acids have

A

NH2 and COOH

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4
Q

Formula of glycine

A

H

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5
Q

Formula for alanine

A

CH3

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6
Q

Formula for valine

A

C3H7

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7
Q

What are the element found in amino acids

A

C H O N and some amino acids S

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8
Q

What is the primary structure of an amino acid

A

The number and the sequence of the amino acids in the polypeptide chain

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9
Q

What is a peptide bond and what typed of reaction is it

A

Amino group of one amino acid reacted with carboxylic COOh group of another
VIA CONDENSATION REACTION

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10
Q

What is the secondary structure

A

The regular folding of polypeptide chain held together by hydrogen bonds

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11
Q

What are the two types of secondary structures

A

Alpha helix
Beta sheet

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12
Q

How does the secondary structure work

A

Hydrogen bonds form between a carboxyl group of one amino acid and imino ( NH) group of amino acids in adjacent chains

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13
Q

What is the tertiary structure

A

Further folding of the polypeptide chain to form a precise compact and geometric shape

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14
Q

What bonds are included in the tertiary structure

A

Hydrogen bonds
Disulfide bonds
Ionic bonds
Hydrophobic and hydrophilic interaction

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15
Q

What is the quaternary structure

A

Two or more polypeptide chains

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16
Q

What is a globular protein

A

Protein with a spherical shape that is solvable in water and have metabolic roles

17
Q

Haemoglobin

A

4 polypeptide chains - quaternary structure ( 2 alpha globin and 2 beta globin)
Conjugated protein has a prosthetic group attached to each polypeptide chain
Four prosthetic group in haemoglobin called haem groups and contain an iron ion ( fe2+)
One oxygen molecules binds to each haem group for transport

18
Q

Insulin

A

Two polypeptide joined by disulfide links
Shape of insulin allowed it to specifically bind to receptors on cell membrane to reduce blood glucose
Hydrophilic R groups on the outside soluble in water
Allows insulin to disslove in water

19
Q

Pepsin

A

Primary structure has few basic r groups preventing tertiary structure from being affected by low pH
Kept stable by h bonds and disulfide links

20
Q

What is the fibrous protein

A

Very long strong insoluble protein with a structural role in organism

21
Q

Collagen

A

3 polypeptide chains
Cross linked to provide mechanical strength
Chains are wound around each other
Chains are held by hydrogen bonds
Hight proportion of glycine

22
Q

Keratin

A

High amounts of cysteine
Amino acid containing sulfur
Disulfide links form between the two polypeptide chains make molecules hard and strong

23
Q

Elastin

A

Crosslinking between poly peptide chains creates a coiled arrange ment

24
Q

Calcium ions

A

Synaptic transmission of nerve impulses
Bone structure
Cofactor in blood clotting
Muscle contraction

25
Sodium
Electrolyte Nerve impulses Reabsorption of water in the kidneys
26
Potassium
Electrolyte Nerve impulse Reabsorption of water in kidney Opening stomata
27
Hydrogen
Hydrogen bond Atp formation Transport of co2 Ph of blood
28
Ammonium
Source of nitrogen Nitrogen cycle Deamination of protein
29
Nitrate
Source of nitrogen Organic bases Nitrogen cycle
30
Hydrogencarbonate
Co2 dissolves in blood Transports Co2 in and out of blood Regulation of blood Ph
31
Chloride
Production of urine Maintains water balance Transports co2 in and out blood Blood ph Hcl in stomach
32
Hydroxide
Involved in regulation of blood ph
33
Phosphate
Components of cell membrane Forms Atp and nucleic acids Components of bone
34
Iron
Transport of oxygen via haemoglobin Transfer of electrons respiration and photosynthesis