Biological Molecules Module 2 Flashcards

1
Q

What is a monomer

A

Small repeating units from which larger molecules are made

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2
Q

What is a polymer + eg

A

Molecules made from lots of monomers eg protein (amino acids), monosaccharides (sugar),

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3
Q

How do you join and separate monomers

A

Hydrolysis: breaking using water
Condensation: 2 monomers join giving water out, forms covalent bond

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4
Q

Properties of water

A

Specific heat capacity
Latent heat
Cohesion
Adhesion

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5
Q

Type of bond and what molecule is water

A

Polar molecule, hydrogen bonds

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6
Q

What are carbohydrates + what do they contain

A

Contain carbon hydrogen oxygen
Known as sacchrides , polysaccharides, monosaccharides

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7
Q

What are polysaccharides + the egs

A

Many monomers linked by glycosidic bonds formed by condensation reactions
Eg: starch, cellulose, glycogen

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8
Q

Blurt cellulose (polysaccharide)

A

In the cell wall of plant ,
Abundant + organic
Beta glucose molecules joined by beta 1-4 glycosidic bonds
Very strong, rope structure

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9
Q

Blurt glycagen (polysacchride)

A

Made of glucose
Similar structure to amylopectin
Alpha 1-6 glycosidic bond that provides branched structure
Stored as small granules in liver, muscle
Less dense
Soluble
Breaks down faster (high metabolic rate)
1-4 horizontal 1-6 branched

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10
Q

Blurt starch (polysaccharide)

A

Insoluble
In plants
Alpha glucose
Structural units: amylopectin, amylose
Amylose: spiral structure, alpha 1-4 glycosidic bond, compact, coils
Amylopectin: branched with 1-6 alpha so molecule can be released easily (1-6 accessible to enzyme).

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11
Q

Explain triglycerides (fatty acids) - lipids

A

Saturated
Glycerol attached to 3 fatty acids
Glycerol is a 3 carbon based molecule
OH (hydroxyl) group bonded to each 3 carbon
Fatty acids is carboxylic (-COOH) and attached to hydrocarbon chain

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12
Q

What is an Esther bond (triglyceride/lipids)

A

Formed by condensation reaction between each of 3 OH groups on glycerol + OH group pf each fatty acids

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13
Q

Explain phospholipids

A

Found in cell membrane
Make ‘bilayer’ structure
One fatty acid molecule replaced by phosphate group - group is hydrophilic and fatty acid tails are hydrophobic

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14
Q

Use of lipids

A

Long term energy store
Thermal insulation
Insulate nerve axons
Protect organs
Hormones

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15
Q

What are lipids

A

Macromolecule - not polymer as subunits can’t repeat indefinitely
Contain carbon, hydrogen, oxygen
Insoluble in h20
Saturated fatty acids = no double bond between C
Monounsaturated fatty acids = one double bond
Polyunsaturated = more than 1 double bond between C in hydrocarbon chain

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16
Q

What’s a polypeptide

A

When amino acids are added to dipeptides
Type of protein

17
Q

Primary structure in protein

A

simple long chain with no intramolecular bonds or interactions only peptide bonds

18
Q

Secondary structure of protein

A

Hydrogen bonds form so molecule folds/coils

19
Q

Tertiary structure of protein

A

Hydrophilic/hydrophobic interactions, hydrogen bonds ionic bonds and disulphile bonds hold molecule together

20
Q

Quaternary structure of protein

A

Hydrophilic + phobic interactions, hydrogen, ionic, disulphide bonds and 2 or more separate polypeptide chains interlinked

21
Q

What’s a disulphide bond

A

Strongest type of bond and between 2 cysteine amino acids and only present if sulphur is present

22
Q

What’s a peptide bond

A

Formed in between individual amino acids molecule

23
Q

Protein blurt

A

Made up of amino acids
It’s the main component of body tissue eg muscle
Biological catalyst
Hormones, receptors, antibodies all proteins
Formed by condensation reaction

24
Q

Shape of protein

A

3 dimensional shape in 2 categories: globular (ball/compact), soluble (hydrophobic ‘r’ group inward and hydrophilic ‘r’ group outside
Fibrous (repeating sequence of amino acid) usually insoluble

25
Haemoglobin protein eg
Globular, transport O2, made of 4 polypeptide 2 alpha chain 2 beta chain, tertiary, soluble in h2o, has non protein haem group with iron ion
26
Insulin protein eg
Globular, peptide hormone released by pancreas, maintains blood glucose levels made of 2 polypeptide chains (A+B) tertiary, joined by disulphide bonds soluble in water
27
Pepsin protein eg
Globular, protease enzyme, made in stomach to digest, single polypeptide chain with symmetrical tertiary structure held together by hydrogen bonds + 2 disulphide bridges, stable in acidity as few groups accept H+ ions
28
Collagen protein eg
Fibrous amino acid bonded by polypeptide bond Made of 3 intertwined alpha helix Every 3rd amino acids in polypeptide chain is glycine as it allows it to close Supportive tissue
29
Elastin protein eg
Fibrous Found in skin where it allows it to stretch/change shape Cross linking so it’s strong
30
Keratin protein eg
Fibrous Found where body needs to be hard Mechanical protection Impermeable barrier to infection + water Lots of cysteine so disulphide bridges between peptide chains Hydrogen bonding