Biological Molecules Word Stimulants Flashcards

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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

A

Proteins

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
Q

Quaternary Protein

A

2+ polypeptide chains

Functions: Haemoglobin, Structures (collagen), enzymes, transport, active transport, hormones, antibodies

26
Q

Biuret Test

A
Proteins
Detects peptide bonds
NaOH solution
\+ dilute CuSO4
Purple = protein
Blue = NA
27
Q

Enzyme Catalyst

A

Lowers activation energy in reactions
Alters rate
Effective in small amounts
Involved but uncnaged

28
Q

Enzyme Substrate Complex

A

Specific

Substrate hydrolysed

29
Q

Induced Fit Model

A

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
Q

Lock and Key

A

Old
Unfavoured theory
Flexible not fixed shape

31
Q

Factors effecting

A

pH
Temp
Conc

32
Q

pH

A

Amalyse - pH 7 - mouth
Pepson - pH 2
Sucrose - pH 4.5

33
Q

Temp

A

Denatures at high temps +40c
Permanent change
Hydrogen Bonds

34
Q

Concentration

A

Substrate/enzyme

Constant if all enzymes occupied

35
Q

Competitive Inhibition

A

Bind to active site
Lengthen time for enzyme-substrate complex
Similar shape to substrate
Penicillin

36
Q

Non Competitive Inhibition

A

Another position
Alters enzyme shape - substrate can’t fit
Increase substrate conc - no effect

37
Q

End Point Inhibition

A

Metabolic pathways disrupted

Negative Feedback

38
Q

Inhibition reversible

A

Not metal poisoning