biological molecules Flashcards

2.1.2 (57 cards)

1
Q

name the 6 unique properties of water

A

1-high melting and boiling point
2-high surface tension
3-high specific heat capacity
4-high latent heat of evaporation
5-solid less dense than liquid
6-excellent solvent

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2
Q

how is waters high melting and boiling point important for living organisms?

A

it helps regulate animals body temperature

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3
Q

how is waters high surface tension important for living organisms?

A

allows organisms to live, float and move around he surface due to it’s cohesion-adhesion

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4
Q

how is waters specific heat capacity and latent heap of evaporation important for living organisms?

A

helps regulate temperature of living organisms and their environment

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5
Q

how is water being less dense in its solid state rather than its liquid state important for living organisms?

A

it keeps lakes, ponds and oceans from freezing over

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6
Q

how is water being an excellent solvent important for organisms?

A

it helps cells transport and use substances/nutrients due to its polar nature and being able to bind to ionic substances and dissolve them

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7
Q

what are the three types of carbohydrates called, and group them

A

monosaccharides, disaccharides (simple sugars) and polysaccharides (complex carbohydrates)

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8
Q

explain monosaccharides and their properties

A

-can be hexose(6 C atoms) or pentose(5 C atoms)
-CnH2nO2
-soluble in water, sweet tasting
-e.g glucose, fructose, galactose
-all reducing sugars

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9
Q

explain disaccharides and their properties

A

-formed in condensation reactions, broken in hydrolysis reactions
-soluble in water, sweet tasting
-eg maltose, sucrose and lactose
-some are reducing sugars

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10
Q

explain polysaccharides and their properties

A

-insoluble in water, bitter tasting
-eg glycogen, starch (storage molecules) and cellulose (structural molecule)

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11
Q

what are the two forms starch comes in?

A

amylose and amylopectin

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12
Q

describe amylose

A

-long chain of alpha glucose molecules joined by 1,4 glycosidic bonds
-coiled/helical shape w/ hydrogen bonds
-compact which is useful as its a storage molecule

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13
Q

describe amylopectin

A

-long chain of alpha glucose
-branched structure of 1,4 glycosidic bonds but also 1,6 glycosidic bonds branching off

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14
Q

describe glycogen

A

-animal storage molecule
-branched structure with 1,4 and 1,6 glycosidic bonds

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15
Q

why are glycogen and starch good storage molecules?

A

they are both insoluble so have no effect on the water potential of the cell
they both have a compact shape

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16
Q

describe cellulose

A

-structural carbohydrate which makes up plant cell wall
-Beta glucose polymer
-straight chains of 1,4 glycosidic bonds (each chain is a microtubule which have hydrogen bonds)

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17
Q

what are the three types of lipids/fats

A

-triglycerides
-phospholipids
-cholesterol

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18
Q

what are the three things fatty acids can be

A

-saturated
-monounsaturated
-polyunsaturated

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19
Q

whats the difference between unsaturated or saturated fatty acids?

A

unsaturated- no double bond, liquid at room temp, lower melting and boiling point and contain less energy, either mono or poly (no. of C=C)
saturated- no double bond, solid at room temp, higher melting and boiling point, contain more energy

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20
Q

symbol and example of roles in living organisms of calcium ions

A

Ca2+
nerve impulse transmission
muscle contraction
cofactor for enzymes

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21
Q

symbol and example of role in living organisms of sodium ions

A

Na+
generating nerve impulses
muscle contraction
co-transport of glucose and amino acids

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22
Q

symbol and example of role in living organisms of potassium ions

A

K+
generating nerve impulses
muscle contraction
regulating fluid balance

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23
Q

symbol and example of role in living organisms of hydrogen ions

A

H+
determines pH of solutions
used in photosynthesis reactions

24
Q

symbol and example of role in living organisms of ammonium ions

A

NH4+
source of nitrogen for plants

25
symbol and example of role in living organisms of iron ions
Fe2+ binds to oxygen within haemoglobin
26
symbol and example of role in living organisms of chloride ions
Cl- maintains blood pH in gas exchange cofactor for amylase enzyme
27
symbol and example of role in living organisms of phosphate ions
PO4 3- component of nucleotides and phospholipids bonds store energy in ATP
28
symbol and example of role in living organisms of hydroxide ions
OH- determines the pH of solutions
29
symbol and example of role in living organisms of nitrate ions
NO3- source of nitrogen
30
symbol and example of role in living organisms of hydrogencarbonate
HCO3- maintains blood pH
31
what is the general formula for a carbohydrate
Cx(H2O)y
32
main roles of lipids
-energy supply -structural components -waterproofing -insulation -protection
33
describe phospholipids
-contain a phosphate and glycerol (the hydrophilic head) and 2 fatty acids (the hydrophobic tail) -form a double layered phosphate bilayer in water -formed in condensation reactions and form ester bonds
34
describe cholesterol
-a lipid known as a sterol -used by animal cells to increase stability of cell membrane -polar molecule (OH group is hydrophilic,rest is hydrophobic) -used to make vitamin D, steroid hormones and bile -reduces fluidity in the cell membrane
35
what do amino acids form
dimers (dipeptides) and polymers (polypeptides)
36
what’s the role of proteins
enzymes antibodies transport hormones structural components muscle contraction
37
describe the structure of amino acids
central carbon atom amino group (NH2) carboxyl group (COOH) hydrogen atom (H) on C1 R group
38
what is the test for proteins
add buried regent blue - negative purple - positive
39
what is the test for lipids
add 2cm3 ethanol and distilled water shake cloudy emulsion - positive
40
what is the test for reducing sugars
2cm3 benedict’s regent heat in water bath for 5m negative - blue low conc - green medium conc - orange positive - brick red
41
what is the test for non- reducing sugars
add 2cm3 hydrochloric acid heat in water bath for 5m neutralise with sodium hydrogencarbonate use reducing sugars test
42
what is the test for starch
add a few drops of iodine orange - negative blue/black - positive
43
describe primary structure in proteins
-the sequence of amino acids -form peptide bonds
44
describe secondary structure in proteins
-folding of the sequence of amino acids -alpha helix of beta pleated sheet -hydrogen bonds
45
describe tertiary structure in proteins
-unique 3d shape -hydrogen, ionic, disulphide and hydrophilic/hydrophobic bonds
46
describe quaternary structure in proteins
-multiple polypeptides or prosthetic groups -hydrogen, ionic, disulphide and -hydrophilic/hydrophobic bonds
47
what are globular proteins
-compact, spherical and soluble proteins -have metabolic roles like enzymes, hormones and antibodies -can be conjugated proteins (attached to a non protein prosthetic group, eg lipids, carbohydrates or metal ions) -eg haemoglobin, insulin or amylase
48
describe fibrous proteins
-elongated polypeptide chains usually insoluble in water -tend to have structural roles like keratin, collagen and elastin
49
describe haemoglobin
-globular protein that carries oxygen around the body in RBC’s. -made up of 4 polypeptide chains, so has quaternary structure. 2 are alpha chains, 2 are beta chains. -conjugated protein (each polypeptide chain has a haem group, aka prosthetic group that contains an iron atom -each iron can reversibly bind with one O2 molecule, so a haemoglobin can carry 4 molecules of o2 at once -compact globular structure allowing it to fit inside RBC’s.
50
why are triglycerides and phospholipids described as macromolecules but not polymers ?
they aren’t repeating molecules of the same atoms , they exist alone not joined by covalent bonds
51
what is a triglyceride
a type of lipid containing a glycerol and 3 fatty acid used for energy storage, protection and insulation
52
what is a conjugated protein
a protein with an added non protein substance ( a prosthetic group attached to) -eg haemoglobin
53
describe insulin
-globular protein (hormone) -regulates blood glucose concentration -soluble to travel in bloodstream -specific shape to fit receptors on cell surface membranes of target cells -made of 2 polypeptide chins joined by disulphide bridges -quaternary structure
54
describe amylose
-globular protein (enzyme) -breaks down starch into maltose -made of a single polypeptide chain folded into both alpha-helixes and beta-pleated sheets
55
describe collagen
-fibrous protein -used as a structural component in skin, tendons, teeth, cartilage, bones and walls of blood vessels -made up of 3 polypeptide chains bonded via covalent and hydrogen bonds -quaternary structure -twisted into a rope like structure so provides strength and flexibility
56
describe keratin
-group of fibrous proteins found in hair, skin+nails -lots of cysteine (amino acid) which allows for disulphide bridges to form, making strong, insoluble molecules -can be flexible or rigid, depending on number of disulphide bridges
57
describe elastin
-fibrous protein found in elastic connective tissue eg walls of blood vessels -elastic which allows tissues to expand and then return to original shape