2.1.2 - biological molecules Flashcards

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1
Q

how does hydrogen bonding occur between water molecules?

A

x

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2
Q

water as a solvent

A

x

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3
Q

water as a transport medium

A

x

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4
Q

water as a coolant

A

x

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5
Q

water as a habitat

A

x

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6
Q

roles of water - give example of prokaryotes and eukaryotes

A

x

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7
Q

concept of monomers and molymers

A

x

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8
Q

importance of condensation and hydrolysis reactions

A

x

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9
Q

chemical elements that make up biological molecules

A

carbohydrates: C,H,O
lipids: C,H,O
proteins: C,H,O,N,S

nucleic acids: C,H,O,N,P

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10
Q

ring structure and properties of glucose

A

hexose monosaccharide

difference between a and b glucose molecule

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11
Q

structure of ribose

A

pentose monosaccharide

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12
Q

difference between hexose and pentose monosaccharides

A

x

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13
Q

synthesis and breakdown of a disaccharide and polysaccharide

A

formation and breakage of glycosidic bonds

SUCROSE

LACTOSE

MALTOSE

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14
Q

structure of starch molecules

A

amylose

amylopectin

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15
Q

structure of glycogen molecules

A

x

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16
Q

structure of cellulose molecules

A

x

17
Q

how the structures and properties of glucose, starch, glycogen and cellulose molecules relate to their functions in living organisms

A

x

18
Q

the structure of a triglyceride and a phospholipid as examples of macromolecules

A

outline of saturated and unsaturated fatty acids

19
Q

the synthesis and breakdown of triglycerides by the formation (esterification) and breakage of ester bonds between fatty acids and glycerol

A

x

20
Q

how the properties of triglyceride, phospholipid and cholesterol molecules relate to their functions in living organisms

A

hydrophobic and hydrophilic regions and energy content

AND

illustrated using examples of prokaryotes and eukaryotes

21
Q

general structure of an amino acid

A

x

22
Q

the synthesis and breakdown of dipeptides and polypeptides

A

forma on and breakage of peptide bonds

23
Q

levels of protein structure

A

To include primary, secondary, tertiary and quaternary structure

AND

hydrogen bonding, hydrophobic and hydrophilic interactions, disulfide bonds and ionic bonds

24
Q

the structure and function of globular proteins including a conjugated protein

A

To include haemoglobin as an example of a conjugated protein (globular protein with a prosthe c group), a named enzyme and insulin

An opportunity to use computer modelling to investigate the levels of protein structure within the molecule

25
Q

the properties and functions of fibrous proteins

A

To include collagen, keratin and elastin (no details of structure are required)

26
Q

key inorganic ions that are involved in
biological processes

A

To include the correct chemical symbols for the following cations and anions:

cations: calcium ions (Ca2+), sodium ions (Na+), potassium ions (K+), hydrogen ions (H+), ammonium ions (NH4+)

anions: nitrate (NO3–), hydrogencarbonate (HCO3–), chloride (Cl –), phosphate (PO43–), hydroxide, (OH–).

27
Q

how to carry out and interpret the results of the following chemical tests:

biuret test for proteins

Benedict’s test for reducing and non-reducing sugars

reagent test strips for reducing sugars iodine test for starch

emulsion test for lipids

A

x

28
Q

quantitative methods to determine the concentration of a chemical substance in a solution

A

To include colorimetry and the use of biosensors (an outline only of the mechanism is required)

29
Q

the principles and uses of paper and thin layer chromatography to separate biological molecules / compounds

A

To include calculation of retention (Rf) values.

30
Q

practical investigations to analyse biological solutions using paper or thin layer chromatography.

A

For example the separation of proteins,
carbohydrates, vitamins or nucleic acids