2.1.2 - biological molecules Flashcards

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

17
Q

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

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

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

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
the properties and functions of fibrous proteins
To include collagen, keratin and elastin (no details of structure are required)
26
key inorganic ions that are involved in biological processes
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
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
x
28
quantitative methods to determine the concentration of a chemical substance in a solution
To include colorimetry and the use of biosensors (an outline only of the mechanism is required)
29
the principles and uses of paper and thin layer chromatography to separate biological molecules / compounds
To include calculation of retention (Rf) values.
30
practical investigations to analyse biological solutions using paper or thin layer chromatography.
For example the separation of proteins, carbohydrates, vitamins or nucleic acids