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Biology > Topic 1: Biological Molecules > Flashcards

Topic 1: Biological Molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Monomer

A

Smaller units from which larger molecules are made

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2
Q

Polymer

A

Molecules made from many monomers joined together

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3
Q

E.g of monomers

A

Monosaccharides
Amino acids
Nucleotides

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4
Q

Condensation reaction

A

Joins 2 molecules
With the formation of a chemical bond
Involves the elimination of a water molecule

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5
Q

Hydrolysis reaction

A

Breaks chemical bond between 2 molecules
Involves the use of a.water molecule

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6
Q

E.g of monosaccharides

A

Glucose
Fructose
Galactose

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7
Q

Disaccharides (formed)

A

Condensation reaction between 2 monosaccharides
Formation of a glycosidic bond
Elimination of a water molecule

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8
Q

Glucose + glucose

A

Maltose

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9
Q

Glucose + fructose

A

Sucrose

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10
Q

Glucose + galactose

A

Lactose

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11
Q

2 glucose isomers

A

Alpha and beta glucose

Position of OH and H groups are inverted on C1 (ABBA)

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12
Q

What is an isomer

A

Same chemical formula, different structure

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13
Q

Polysaccharides

A

Condensation of many monomers
examples include starch glycogen and cellulose

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14
Q

Glycogen structure - function

A

Stored form of glucose
Polymer of alpha glucose
1,4 and 1,6 glycosidic bonds
Highly branched structure : increases surface area - more ends for rapid hydrolysis of glycogen into glucose (glucose used in respiration)
Insoluble so doesn’t affect water potential

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15
Q

Starch structure - function

A

Stored form of glucose
Polymer of alpha glucose
-> Amylose and Amylopectin
Amylose: 1,4 glycosidic bonds only. Unbranched; helical structure - compact - good storage molecule (lots of glucose fits into a small space)
Amylopectin: 1,4 and 1,6 glycosidic bonds. Branched - increases surface area - more ends for hydrolysis into glucose

Insoluble so doesn’t affect water potential

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16
Q

Cellulose structure - function

A

Provides structural strength (cell wall)
Polymer of beta glucose
1,4 glycosidic bonds only - forms long straight chains of beta glucose - lie parallel - linked by hydrogen bonds - form fibrils - provides (collective due to large number of H bonds) strength

Insoluble so doesn’t affect water potential

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17
Q

Benedict’s test for reducing sugar

A

Add Benedict’s reagent and heat
Positive: blue to red (precipitate)

18
Q

Non reducing sugar test

A

Add acid (hydrolyses glycosidic bonds)
Then neutralise
Then heat with Benedict’s
Blue to red = positive

19
Q

Concentration of sugar in Benedict’s test

A

Use colorimeter
Or observe with own eyes. Red = strong concentration, yellow = moderate, green = weak concentration

20
Q

Colorimetry in food tests

A

Make standard solutions with known concentrations
Record absorbable and plot calibration curve

Make your own samples, record absorbable of unknown samples and use the calibration curve to determine their concentration

21
Q

Protein

A

Polymer made up of amino acid monomers

22
Q

Dipeptide

A

2 amino acids join together in condensation reaction
Peptide bond forms
Elimination of a water molecule

23
Q

Amino acid general structure

A

Nh2 (amine group) R, C, H, COOH (carboxyl group)

24
Q

Primary structure of a protein

A

The sequence of amino acids in a polypeptide chain

25
Q

Secondary structure of a protein

A

Folding / twisting
Beta pleated sheet / alpha helix
Hydrogen bonds

26
Q

Tertiary structure of a protein

A

Further folding
Unique 3D shape
Hydrogen, ionic, disulfide bonds

27
Q

Quaternary structure of a protein

A

More than one polypeptide chain
Functional Protein

28
Q

What determines the sequence of amino acids in a polypeptide chain?

A

Base sequence of DNA (a triplet: 3 bases codes for a specific amino acid)

29
Q

Why is primary structure important

A

Determines where bonds form (tertiary structure)
Determines unique 3D shape

30
Q

Explain how a mutation can prevent the formation of antigen-antibody complex

A

Mutation changes sequence of amino acids (primary structure)
- If different sequence of amino acids: bonds form in different locations, get a different 3D shape.
- So antibody and antigen no longer have complementary shape.

31
Q

Biuret test

A

Biuret solution tests for proteins

  • Add sodium hydroxide (to make it alkaline)
  • Then add copper (II) sulfate
    Positive result = colour change from blue to purple.
32
Q

Enzymes

A

Proteins
Biological catalysts - speed up rate of reactions.

33
Q

Active site

A

The part of the enzyme where the substrate will bind

34
Q

Substrate

A

The substance that the enzyme interacts with, binds to the active site

35
Q

Specificity of enzymes

A

Only one substrate fits in active site (complementary in shape)
Active site shape determined by tertiary structure, which is determined by primary protein structure
If substrate is complementary, E-S complex is for,Ed and reaction is catalysed

36
Q

If the tertiary structure of the protein is altered, the active site changes shape. What does this mean?

A

The substrate is no longer complementary in shape so won’t fit in active site
E-S complex cannot be formed
Enzyme is non functional, cannot catalyse reaction

37
Q

How can a mutation impact the functioning of an enzyme?

A

Mutation can happen in a gene which alters the primary structure of a protein
If primary structure changes, tertiary structure could change, meaning an E-S complex can no longer be formed and the enzyme is non functional.

38
Q

How do enzymes lower activation energy?

A

Fitting into the active site puts a strain on bonds in the substrate -> products made more easily

39
Q

What is activation energy?

A

The amount of energy required for a reaction to start

40
Q

Why is the fact that enzymes lower activation energy beneficial?

A

Reactions can happen at a lower temperature than without an enzyme
- this is because increasing temperature increases kinetic energy, and enzymes lower activation energy so therefore a lower temperature can be used.

41
Q

Induced fit vs lock and key

A

Induced fit is accepted rather than lock and key.
Induced fit: substrate has a complementary shape to the active site, but the active site also changes shape slightly when the substrate binds.

Biology (9 decks)

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