Biological Molecules Word Stimulants Flashcards

(38 cards)

1
Q

Glucose

A

Alpha (OH same)

Beta (OH different)

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2
Q

Glycosidic Bond

A

Condensation Reaction

Carbohydrates

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3
Q

Condensation Reaction

A

H2O produced

Monosaccharides > Disaccharides > Polysaccharides

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4
Q

Hydrolysis

A

H2O used

Polysaccharides > Disaccharides > Monosaccharides

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5
Q

Maltose

A

Alpha Glucose + Alpha Glucose

Reducing Sugar

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6
Q

Sucrose

A

Alpha Glucose + Beta Fructose

Reducing Sugar

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7
Q

Lactose

A

Alpha Glucose + Galactose

Non Reducing Sugar

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8
Q

Reducing Sugars

A
All monosaccharides+ some di
Benedicts solution
Heat
Blue - non, Green - low, Red - high
Colourimetry
Calibration Curve
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9
Q

Non Reducing Sugars

A

Test for reducing
Dilute HCl - Di to mono
Sodium hydrocarbonate - neutralise - pH paper test
Test reducing

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10
Q

Starch

A

Plants
Coiled - Helix, alpha glucose
1-6/1-4 glycosidic bonds
Branched - Enzymes easily hydrolyse into monomers (respiration, easily transported)
Excellent Storage - Not v soluble, large (doesn’t diffuse out of cells), dense
Seeds, grain
Test - Potassium Iodine, heat, yellow/orange > blue/black

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11
Q

Glucogen

A

Animal+Fungi
Coiled - alpha glucose
1-6 glycosidic bonds
Highly Branched - Enzymes easily hydrolyse into monomers (respiration, easily transported)
Storage - Compact; shorter; less dense; more soluble (still insoluble - doesn’t diffuse out of cells)
Animals higher metabolic rate
Granuales

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12
Q

Cellulose

A

Plants
Linear - beta glucose (rotates 180)
Straight, Unbranched
H bonds between layers - High tense strength
Rigidity in cell walls - prevent bursting (osmosis)
Microfibrils > Fibres

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13
Q

Triglycerides

A

Glycerol + 3 fatty acids
Condensation reaction
Saturated/unsaturated
ESTER Bond

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14
Q

Phospholipids

A

Glycerol + 2 fatty acids + Phosphate group
Hydrophilic - dissolves in h2o, P group
Hydrophoblic - does not dissolve in h2o, fatty acids
Bilayer in cell membrane
Glycolipids (+carbohydrates) recognition sites

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15
Q

Emulsion Test

A

Mix Ethanol + test material
Shake - dissolve lipids
Add h2o + mix
Milky white emulsion = lipids

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16
Q

Lipid Properties

A
Insoluble in h2o
Store chemical energy (fats and oils)
Readily hydrolysed
Used in respiration (release o2, glucose short supply)
Pass through phospholipid bilayer
Low energy : mass ratio - good storage
17
Q

Lipid Uses

A

Energy Store - insoluble in h2o, long term resource
Insulation - fat poor heat conductor, fatty mylein sheath
Protection - Fat around organs
Structural - phospholipids - cell membranes
Molecules - steroids, hormones

18
Q

Peptide Bonds

19
Q

Amino Acid structure

A

C - Amine, H, COOH, R (carbon side chain)

20 types

20
Q

Dipeptide/polypeptide

A

2/many amino acids combine
Condensation reaction
Peptide Bond

21
Q

Primary Protein

A

Amino acid sequence (polypeptide chain)
Unique
Determines structure, functions, chemical properties

22
Q

Secondary Protein

A

Hydrogen Bonding (C=O + NH)
A helix - Twists chain, coils, one polypeptide chain
Beta Pleated Sheet - different parallel chains, folded chain

23
Q

Tertiary Protein

A

A helixes + Beta pleated sheets of many proteins
Fold and bend into shape
Weak covalent bonds (H bonds, ionic interactions COOH+NH2, Van Der Waals - non polar R groups)
Strong covalent bonds (Disulfide bridges)
Flexible
Respond to changes in pH + temp

24
Q

Disulfide Bridges

A

Tertiary Structure

Broken by pH

25
Quaternary Protein
2+ polypeptide chains | Functions: Haemoglobin, Structures (collagen), enzymes, transport, active transport, hormones, antibodies
26
Biuret Test
``` Proteins Detects peptide bonds NaOH solution + dilute CuSO4 Purple = protein Blue = NA ```
27
Enzyme Catalyst
Lowers activation energy in reactions Alters rate Effective in small amounts Involved but uncnaged
28
Enzyme Substrate Complex
Specific | Substrate hydrolysed
29
Induced Fit Model
Complementary active sites (H Bonds maintain shape; small no. of aa depressions) Tertiary structure of proteins Bonds temporarily (with aa on substrate) Enzyme flexible - to fit substrate Strain on substrate (distorts bond-lowers Ea)
30
Lock and Key
Old Unfavoured theory Flexible not fixed shape
31
Factors effecting
pH Temp Conc
32
pH
Amalyse - pH 7 - mouth Pepson - pH 2 Sucrose - pH 4.5
33
Temp
Denatures at high temps +40c Permanent change Hydrogen Bonds
34
Concentration
Substrate/enzyme | Constant if all enzymes occupied
35
Competitive Inhibition
Bind to active site Lengthen time for enzyme-substrate complex Similar shape to substrate Penicillin
36
Non Competitive Inhibition
Another position Alters enzyme shape - substrate can't fit Increase substrate conc - no effect
37
End Point Inhibition
Metabolic pathways disrupted | Negative Feedback
38
Inhibition reversible
Not metal poisoning