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Biology > Biological Molecules > Flashcards

Biological Molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What is a monomer?

A

Small basic mollecular unit

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2
Q

What is a polymer?

A

large, complex molecule made of monomers of the same type

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3
Q

What is an isomer? And an example

A

Two or more compounds with the same formula but a different arrangement of atoms. Example is alpha and beta glucose

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4
Q

What is a condensation reaction?

A

Joins molecules together and forms water

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5
Q

What is a hydrolysis reaction?

A

Chemical reaction where water is used to break down a compound

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6
Q

Name all 3 monosaccharides

A

Glucose
Fructose
Galactose

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7
Q

Name the two pentose sugars

A

Deoxiribose

Ribose

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8
Q

Name all 3 Disaccharides and the monosaccharides that make them up

A

Sucrose - glucose+fructose
Lactose - glucose+galactose
Maltose- glucose+glucose

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9
Q

Name the reactions that break apart and join monosaccharides

A

Hydrolysis reaction - breaks apart

Condensation reaction - joins

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10
Q

Outline the structure and function of cellulose

A 
Made of B glucose
1-4 glycosidic bonds
chains form microfibrils, then form macrofibrils
glued together by pectin
form cell walls in plants
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11
Q

Outline the structure and function of Starch

A 
ENERGY STORE IN PLANTS
Amylose:
A glucose
unbranched and coiled
1-4 glycosidic bonds
Amylopectin:
A glucose 
branched due to 1-4 and 1-6 glycosidic bonds
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12
Q

Outline the structure and function of Glycogen

A

ENERGY STORE IN ANIMALS
A glucose
very branched with 1-4 and 1-6 glycosidic bonds

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13
Q

Names 4 advantages of using polysaccharides as enery stores

A

large molecule- cannot diffuse out of cell
insoluble- doesnt affect water potential of the cell and therefore the osmotic pressure
Compact- effecient storage
easily broken down in hydrolysis- readily accessible energy

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14
Q

Name 4 functions of lipids

A 
cell membrane structure
hormones
energy store
thermal insulation
machanical protection
electrical insulation in nerves
waterproofing and boyancy
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15
Q

What is the bond formed in lipids?

A

Ester bond

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16
Q

How are ester bonds formed?

A

Condensation reaction

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17
Q

Describe the structure and function of a triglyceride

A

Glycerol and 3 fatty acids

Main energy source for the body when extra colories arent needed

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18
Q

Where do triglycerides come from?

A

foods like butter, oils and other fats

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19
Q

What is the function of glycerol?

A

Energy store

framework for fatty acids to be added to

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20
Q

What is the function of fatty acids?

A

Used for energy in cells when there is no glucose available

21
Q

What state are saturated and unsaturated fatty acids in at room temperature?

A

Saturated fatty acids are solid

Unsaturated fatty acids are liquid

22
Q

Which fatty acid, saturated or unsaturated, has a double bond between carbon atoms

A

unsaturated

23
Q

What can saturated fatty acids lead to?

A

Increase in cholesterol and LDL’s (low density lypoproteins)

24
Q

Are lipids soluble?

A

No

25
Q

Describe the structure of a phospholipid and its function

A

Hydrophillic head, hydrophobic tail
two fatty acid chains attached to a glycerol with a phosphate group
forms cell membrane
controls what goes in and out of cell

26
Q

Describe the structure and function of cholesterol

A

4 carbon rings
hydrphobic and hydrphillic ends
Sits amongst hydrophobic hydrocarbon chains in phospholipid bilayer, adding strength by reducing fluidity
Hormones, oestrogen, testosterone and vitamin D as examples

27
Q

What makes a molecule typically hydrophobic?

A

Made from carbons surrounded by hydrogen atoms

28
Q

What are liquid triglycerides and solid triglycerides known as?

A

Solid triglycerides are fats

Liquid triglycerides are oils

29
Q

What bond forms between amino acids?

A

peptide bonds

30
Q

How are peptide bonds formed?

A

condensation reaction

31
Q

What atoms do all amino acids contain?

A

Oxygen, hydrogen, nitrogen and carbon

32
Q

What are enzymes that break peptide bonds called?

A

Proteases

33
Q

Why may chains on amino acids be broken down?

A

Digestion- to from new amino acids for use to make new proteins
Hormones- to make sure the effects of homones arent permanent

34
Q

Describe the primary structure of a protein and what bonds are used

A

Sequence of amino acids

Has only peptide bonds

35
Q

Describe the secondary structure of a protein and what bonds are used

A

Long chains of amino acids fold into regions with repeating patterns, alpha helix and beta pleated sheet
Contains peptide and hydrogen bonds

36
Q

Describe the tertiary structure of a protein and what bonds are used

A

Final 3D resting shape of the protein
Contains peptide bonds, hydrogen bonds, hydrophobic and hydrophyllic interactions between polar and non polar R groups, ionic bonds between opposite charged R groups and disulfide bonds/bridges.

37
Q

Describe the quaternary structure of a protein and what bonds are used

A

More than one ploypeptide chain. Haemoglobin for example.
Contains peptide bonds, hydrogen bonds, hydrophobic and hydrophyllic interactions between polar and non polar R groups, ionic bonds between opposite charged R groups and disulfide bonds/bridges.

38
Q

Describe Ab initio protein modelling

A

Model is built based on the physical and electrical properties of the atoms in each amino acid in the sequence

39
Q

Describe comparative protein modelling

A

One way is protein threading, which scans amino acid sequences against a database of solved structures and produces a set of possible models which would match that sequence

40
Q

Name 3 fibrous proteins

A

Keratin
Elastin
Collagen

41
Q

Name 3 globular proteins

A

Insulin
Catalase
Haemoglobin

42
Q

Where is keratin found and what is its function?

A

Founds in hair, skin and nails. Number of disulfide bonds determines flexiility

43
Q

Where is elastin found and what is its function?

A

Found in walls of blood vessels and alveoli. Has a quaternary structure and can expand and return to normal shape

44
Q

Where is collagen found and what is its function?

A

Used as connective tissue in ligaments, skin, tendons and the nervous system and is very flexible

45
Q

What is the function of insulin?

A

Used to regulate blood-glucose levels and is soluble

46
Q

What is the structure and function of catalase?

A

Breaks down hydrogen peroxide into water and oxygen. Has 4 haem prosthestic groups and a quaternary structure

47
Q

What is the structure and function of haemoglobin?

A

Has 2 alpha and 2 beta sub units, each with a prosthetic haem group. These contain iron which can reversably bind to oxygen and transport it around the body

48
Q

What are cations?

A

positively charged ions

Biology (4 decks)

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