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Biology > Proteins > Flashcards

Proteins Flashcards

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AP® Biology flashcards Biology 101 flashcards
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
Q

Sodium

A

Electrolyte
Nerve impulses
Reabsorption of water in the kidneys

26
Q

Potassium

A

Electrolyte
Nerve impulse
Reabsorption of water in kidney
Opening stomata

27
Q

Hydrogen

A

Hydrogen bond
Atp formation
Transport of co2
Ph of blood

28
Q

Ammonium

A

Source of nitrogen
Nitrogen cycle
Deamination of protein

29
Q

Nitrate

A

Source of nitrogen
Organic bases
Nitrogen cycle

30
Q

Hydrogencarbonate

A

Co2 dissolves in blood
Transports Co2 in and out of blood
Regulation of blood Ph

31
Q

Chloride

A

Production of urine
Maintains water balance
Transports co2 in and out blood
Blood ph
Hcl in stomach

32
Q

Hydroxide

A

Involved in regulation of blood ph

33
Q

Phosphate

A

Components of cell membrane
Forms Atp and nucleic acids
Components of bone

34
Q

Iron

A

Transport of oxygen via haemoglobin
Transfer of electrons respiration and photosynthesis

Biology (12 decks)

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