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Biology 785 > Biological molecules > Flashcards

Biological molecules Flashcards

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1
Q

Functions of carbohydrates

A 
Energy source 
Structural components 
Storage compounds
Transport 
Cell recognition 
Metabolites
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2
Q

Test for carbs - reducing sugar

A

1cm3 Benedictus solution with 2cm3 of carb solution
Water bath 5mins 60C

Brick red +
To
Blue -

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3
Q

Test for non reducing sugars

A 
Carry out Benedictus test 
If negative 1cm3 of dilute HCl
Water bath 5mins 
Neutralise 1cm3 NaOH
retest with Benedicts
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4
Q

Test for carbs (i)

A

3 drops of iodine In 2cm3 of carb solution
Make sure solution is cold
Blue black +
Brown -

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5
Q

2 types of glucose and the difference

A

Alpha - H
OH

Beta - OH
H

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6
Q

Sucrose
Lactose
Made from?

A

Glucose and fructose

Glucose and galactose

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7
Q

Polysaccharides

A

Long chain of monosaccharides bonded together by glycosidic bonds via condensation reactions

Large stable and insoluble

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8
Q

Most common polysaccharides

A

Glycogen
Starch
Cellulose

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9
Q

Main storage polysaccharides in plants

A

Amylose
Helix
Forms starch w/ 1-4 glycosidic bonds
Compact and long term

Amylopectin
Branched so quicker to hydrolyse to glucose
1-4 and 1-6 glycosidic binds to for starch

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10
Q

2 types of glucose as polysaccharides are

A

Glycogen -a
Branched, compact, insoluble,
Cellulose - ß every other glucose molecule flipped so atoms line up to form H2O
Branched, meshed layered network, permeable and strong

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11
Q

Triglycerides are lipids made from

A

1 glycerol and 3 fatty acids ( 14-22 C atoms)

Fats have single bonds
Oils have1 or more double bonds

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12
Q

Phospholipids made up of

A

1 glycerol
1 phosphate group makes it polar hydrophilic PO4-3
2 fatty acids hydrophobic

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13
Q

Phospholipids form

A

Bilayers in membranes
Droplets called micelles ( in water )
Bilayer droplet called a liposome

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14
Q

Test for lipids

A

2cm3 of sample and 5cm3 of ethanol
Shake
Add 5cm3 of water and shake
If a lipid is present it will dissolve and form a cloud white emulsion

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15
Q

Proteins

A

Made of amino acids (20 different types)
NH3,CHR,COOH
R group is what makes the amino acids different

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16
Q

Primary protein
Secondary protein
Tertiary protein
Quaternary protein

A
  • Order of amino acids
  • a helix ( coil to form filaments) or ß pleated sheet ( run in same or opposite direction)
  • a and ß (secondary) bonded together by hydrogen bonds, ionic bonds and disulphide bridges ( covalent bonds between sulphur) poly peptide chain
  • 2 or more polypeptide chains linked together either
    Globular - tightly folded into a spherical like shape
    Fibrous - cross linked and intervals to form fibres and sheets
17
Q

Test for proteins

A

Sample of solution and an equal amount of NaOH
Few drops of copper(ii) sulfate
Purple +
Blue -

18
Q

Enzymes

A

Globular Proteins that change the rate of reaction by dec the activation energy

19
Q

Metabolic rate

A

The rate of catabolic and anabolic reactions that can be sped up by enzymes

20
Q

Factors that may effect rate of reaction

A

Enzyme conc - as conc inc rate inc until substrate is limiting and ot no longer inc
Substrate conc -as conc inc rate inc until enzymes is limiting and rate does nit inc
Temp - not enough energy, optimum ( varies ), enzyme denatures
pH - as you move away from optimum ( varies) enzyme denatures however can return to normal when optimum is met

21
Q

Why pH effects the rate of reaction w/ enzymes

A
  • Change in pH alters con of H+ or OH- ions
  • This change will disrupt the H bonds holding together 2nd and 3rd protein structure and the Ionic bonds in the 3rd
  • causes the 3D structure to change therefore active site changes
  • prevents formation of substrate-enzyme complex as enzyme is denatures
22
Q

Mechanism for enzyme action

A

Induced fit hypothesis
Enzyme active site changes shape slightly to fit the substrate which puts strain on the substrate molecule
Strain distorts and particular bond and therefore lowers the activation energy

23
Q

Induced fit is better than lock and key because…

A

Shows how other molecules can effect enzyme activity

Shows how enzymes lower activation energy

24
Q

Enzyme inhibition - competitive inhibitor

A

Competes with the substrate fir position on active site

Of the amount of inhibitor is fixed the % of inhibition can be dec by inc the substrate conc

25
Q

Enzyme inhibition - non competitive inhibitor

A

Bonds to allosteric site so active site becomes denatured

26
Q

ATP

A 
Small simple molecule 
Used to power most energy requiring cellular reactions
 Made of 
Adenine 
Ribose (pentose sugar)
3 phosphate groups
27
Q

Hydrolysis of ATP

A

Releases energy and forms ADP and a Pi ion (that can be used to phosphorylate other compounds to make them more reactive)

Reversible reaction however the resynthesis is catalysed by ATP synthase I’m respiration/photosynthesis

28
Q

Nucleotides

A

Make up DNA and RNA
made up of one of 4 bases ( adenine, guanine, cytosine thymine[DNA]\uracil[RNA])
Phosphate group
Pentose sugar deoxyribose DNA or ribose RNA

29
Q

Joining of nucleotides to dinucleotide or polynucleotide

A

Polymerise to form phsophodiester bonds

Either 5” (phosphate up) or 3” (phosphate down) DNA is 1 of each(double helix) RNA is single helix

30
Q

A-T/U

C-G

A

Complementary base pairing
A-T form 2 H bonds
C-G form 3 H bonds
Allows for variation

31
Q

DNA structure and function

A

Double helix -coiled and compact protects H Bonds and bases
H bonds - can easily be broken to separate strands of DNA replication
Large molecule - lost can be stored in a small volume when coiled
Sugar phosphate backbone - strong and stable so genetic info can be passed through generations

32
Q

History of DNA

A

Erwin Chargaff - conc of C to G was proportional to conc of A to T
Rosalind Franklin and Wilkins - helical structure
Watson and crick - assimilated, dna was 2 polynucleotide chains
Gaps were wither major or minor

Biology 785 (6 decks)

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