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Biology AS Level > BIO MOLECULES p2 > Flashcards

BIO MOLECULES p2 Flashcards

1
Q

Hydrogen bond + what happends if iodine amyolse complex heated at very high temp

A
  • Via condensation reaction between O2 + H+
  • Between electro- and electro+
  • H+ break
  • Helix breaks
  • Iodine released
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2
Q

DISULPHIDE BOND

A

A STRONG COVALENT bond formed between SULFUR atoms of R groups of 2 cysteine AA.

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3
Q

GLYCOSIDIC BOND

A

A covalent bond formed when 2 carbohydrate mol joined via condensation reaction

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4
Q

General formula for cellulose

A

(C6H10O5)n

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5
Q

Collagen

A

1) structural FIBROUS protein
2) found in tendons, skin, cartilage = NOT parallel gives strength in diff directions

3) 3 polypeptide chains
- glycine allows tight coiling of pp= triple helix
- forms H+ w/ C=O of other pp in triple helix
4) Primary ss held via peptide bonds

6) every 3rd AA
- covalent bonds between R groups + STRONG

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6
Q

Fibrous proteins// collagen

A

1) proteins that form long strands/polypeptide chain
2) INSOLUABLE
3) have structural roles
4) eg, actin, myosin, keratin, collagen

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7
Q

Quaternary structure

A

2/++ polypeptides
- held together by 4 bonds
- collagen = fibrous + 3 polypep chain
- hemoglobin = globular + 4 polypep chain
- multiple polypeptide chains and/or non-protein (prosthetic) groups link = LARGE PROTEINS

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8
Q

Hemoglobin

A
  1. PRIMARY SS= sequence of AA joined by peptide bonds
  2. SECONDARY SS= alpha helix + B pleated sheets + folding + H+
  3. TERTIARY SS= polypep chain further coiling
    - 3 bond interactions: disulphide, ionic, polar hydrophilic R-groups on outside of mol/ hydrophobic R-groups on inside

4.QUANT SS= 4 polypeptide chains , 2 ALPHA- globin + 2 BETA-globin
- 1 haem group per polypeptide, 4 heams per mol
4. Haem/prosthetic group contains Fe2+ combines w 1 oxygen = oxyhemoglobin (cooperative binding)

  1. Responsible for color of Hb = Purple–> bright red when oxidized
    - spherical
    - soluble / forms H+ w water
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9
Q

Primary structure

A
  • seuquence of amino acids bonded via covalent peptide bonds
  • specific for each protein
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10
Q

molecular formula of maltose + sucrose

A

C12H22O11

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11
Q

formula of ribose

A

C5H10O5

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12
Q

PROTEIN TEST

A

-sample of the sol placed in a test tube
- equal vol of sodium hydroxide solution is added at room temp
- ++ Biuret ‘reagent added & mixed
- blue to purple = PRESENT (peptide bonds detected)

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13
Q

What is the name of the group that all fatty acids have?

A
  • Carboxyl group (-COOH)
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14
Q

What is the effect of double bonds in hydrocarbon chains?

A

-mol bend = prevents close packing
- so liquids at room temperature

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15
Q

How is the structure of triglycerides related to their properties?

A
  • HIGH ratio of C:H = good energy source
    -LOW mass:energy ratio = energy stored in small vol
  • large & non-polar= insoluble in water- no effect on water potential
  • HIGH ratio of O:H = release water
  • 1 glycerol and 3 fatty acid
  • via condenstaion reaction to make ester bond (OH)
  • carboxylic group (COOH) form
  • enzyme lipase
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16
Q

Name a substance that lipids are soluble in

A

ethanol

17
Q

Name the constituent monomers of maltose

A

glucose + glucose via condensation reaction (monosaccaride)

18
Q

Name the constituent monomers of lactose

A

glucose and galacctose via condensation reaction (monosaccaride)

19
Q

which mol contain C=O bonds

A
  • AA
  • Fatty acids
  • Proteins
  • glucose (structural)
20
Q

which carb likely to give brick red color when heated w benedicts reganret sol

A
  • fructose
21
Q

features of one mol of sucrose when hydrolyzed

A
  • 2 mol of reducing sugar produced
  • 1 mol of water produced
22
Q

which bonds are last to break when enzyme is heated

A
  • disulphide
23
Q

glycerol

A

C3H808 formula

24
Q

state 2 structural differences between fructose + sucrose

A

Fructose
- no glycosidic bond
- beta glucose
- C6H12O6
- monosaccharide (one sugar unit)
- single ring
- reducing end

Sucrose
- glycosidic bond
- disaccharide (2 sugar units)
- C12H22O11
- non reducing end
- two rings

25
Q

describe physical properties of water allow survival of orgnisms at range of temps

A

HIGH LATENT HEAT OF VAPORISATION = removal of large quantities of thermal energy by evap/cooling effect
- Evap is cooling mechanims e.g sweating or reduce rate of water loss by transpiration

HSHC = large amount of energy needed to raise temp by 1ºC
- thermally stable for aquatic life e.g salmon
- use less energy for thermal regulation as internal temp changes slowly

High density /Ice less dense than water = surface provides habitat for organisms/floatation

ST= habitat for invertebrates e.g water striders

Cohesion/adhesion = transpirational pull of water up xylem via adhesion between water mol + cellulose CW

Solvent= medium for metabolic/chemical reactions

Water insulated = doesnt freeze aquatic life

Transparent = allows photosyntheiss for aquatic plants

26
Q

describe how conc of reducing sugar can be measured using colorimeter

A
  • standard cocn of reducing sugar
  • heat w equal vol Benedicts sol each time
  • changes to green/yellow/orange/brown/brick red
  • remove ppt/obtain filtrate
  • calibrate/zero
  • using a blank/water
  • use red filter
  • reading of transmission/absorbance
  • more tranmsission = more sugar present
  • obtain calibration curve + plot against sugar conc
27
Q

GLYCOGEN VS CELLULOSE

A

G then C

  • NO H+ vs H+
  • 1,4 and 1,6 GB vs 1,4 GB
  • branched vs straight
  • NO fibres vs fibrils
28
Q

describe how 2nd AA would bond to cysteine in forming primary ss of protein

A
  • peptide bonds form betwen amine group of 1 AA and OH of carboxyl group on another AA
    -Via condensation reaction + water created
29
Q

explain how to determine rate of hydrolysis of starch

A
  • take sample at regular time intervals
  • test for presence of starch//reducing sugar +++ iodine in potassium iodide solution OR Bendicts to sample
  • observe color change to determine end point= continue until no blue black color OR until brick red
  • TIME TAKEN TO REACH END POINT
  • use colorimeter for more quantitative/precise results
  • plot graph of amount of starch remaining
30
Q

[GLOBULAR VS FIBROUS USEING EXAMPLE

A

FIBROUS:
- Long chain forms H+ w adjacent chains
- Insoluable = few hydrophilic groups
- Strong + have ss role
- collagen has high prop of glycine
- collagen forms crosslinks/Covalent bonds between mol
- ends of mol staggered to AVOID WEAK POINTS
- collagen froms skin/bone/cartlidge

GLOBULAR:
- spherical + soluble
- hydrophilloic R groups facing exterior FORM H+ w water
- Hb carries oxygen
- Hb contains prosthetic group/Fe2+ to bind w O2
- polypep within HB have tertiary ss = ball shape

31
Q

micelle

A

Spherical structures with hydrophobic tails inside and hydrophilic heads outside.

32
Q

If the difference in electronegativity across a bond is > 0.4 (gretater)…its

A

POLAR

33
Q
A

Biology AS Level (12 decks)

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