Biological molecules Flashcards

1
Q

Properties of water

A

-surface tension
- adhesion
- cohesion
- specific heat capacity
- latent heat of evaporation
- solvent for polar molecules
- density

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2
Q

Monosaccharides

A

individual units of sugar

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3
Q

Disaccharides

A

Two monosaccharides bonded- a dimer.

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4
Q

difference between alpha and beta glucose

A

alpha glucose has hydrogen above OH on the first carbon. Beta glucose has the reverse.

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5
Q

lactose

A

Galactose and glucose

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6
Q

Maltose

A

Alpha glucose and Alpha glucose

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7
Q

Sucrose

A

Fructose and glucose

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8
Q

Reducing sugar

A

a sugar that donates electrons (to the benedicts solution)

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9
Q

Glycogen- monomer

A

Alpha glucose

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10
Q

Glycogen bonds

A

1,4 1,6

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11
Q

Glycogen structure

A

Branched, more energy from hydrolysis

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12
Q

amylose monomer

A

Alpha glucose

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13
Q

Amylose bonds

A

1,4

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14
Q

Amylose structure

A

complex helix, unbranched

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15
Q

Amylopectin monomer

A

Alpha glucose

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16
Q

Amylopectin bonds

A

1,4 1,6

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17
Q

Amylopectin structure

A

Branched, less so than glycogen

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18
Q

Cellulose monomer

A

Beta glucose

19
Q

Cellulose bonds

A

1,4

20
Q

Cellusose structure

A

unbranched, hydrogen bonds between strands.
microfibrils- macrofibrils- cellulose fibre

21
Q

Fatty acids structure

A

Methyl group. hydrocarbon chain. carboxylic group.
some saturated, some unsaturated.

22
Q

Glycerol structure

A

3 carbon atoms
3 OH
The rest are carbon atoms

23
Q

Triglyceride

A

3 fatty acids, one glycerol. joined together by ester bonds.

24
Q

Glycosidic bonds

A

Bonds between monosaccharides

25
Q

Phospholipids

A

like a triglyceride but instead of 3 fatty acids, has 2 fatty acids and a phosphate group attached to the glycerol.

26
Q

Amino acid structure

A

An amine end (NHH) and a carboxyl end. has an R group, which is a variable region that changes based on which amino acid it is.

27
Q

peptide bond

A

Bond between amino acids

28
Q

Primary structure

A

A chain of sequenced amino acids, joined by peptide bonds.

29
Q

Secondary structure

A

Hydrogen bonds begin to form, joining parts of the chain. (alpha helix or beta pleated sheets)

30
Q

Tertiary structure

A

Disulphide bridges, ionic bonds between R groups. This folds the polypeptide into a 3 dimensional protien.

31
Q

Quarternary structure

A

Two or more tertiary structures together. protiens like haemoglobin, insulin ect

32
Q

Conjugated protein

A

A protein with another chemical group (a prosthetic group) that forms part of the protien.

33
Q

list the order of magnitude of cellulose fibre…(ascending order)

A
  • cellulose
  • microfibrils
  • macro fibrils
  • cellulose fibre
34
Q

What are biosensors?

A

Biological componants used to determine presence and concentration of biological molecules.

35
Q

What do we call “ the compound under investigation”?

A

The analyte

36
Q

What binds to the analyte in a biosensor? What does it do?

A

a protien or a single strand of DNA. It interacts with the analyte.

37
Q

What happens after mollecular recognition in a biosensor?

A
  • The interaction between anayte and protien or DNA causes a change across transducer.
  • the transducer will produce a response.
38
Q

What sort of responses could a transducer induce?

A
  • release an immobalised dye on a test strip.
  • release an electric current.
39
Q

roles of lipids- not energy(4)

A
  • electrical impulse insulation for impulse transmission
  • hormone production
  • membrane formation
  • water proofing (hydrophobic)
40
Q

roles if lipids- energy (3)

A
  • thermal insulation to reduce heat loss
  • cushioning to protect vital organs
  • buoyancy for aquatic animals
41
Q

Talk about the structure of fibrous protiens… 4 things

A

high proportion of hydrophobic R groups
limited range of amino acids
Small R groups
primary structure usually quite repetitive.

42
Q

Talk about the structure of globular proteins…

A

Hydrophobic areas pointing inwards.
Roughly a spherical shape.

43
Q

Name for a protein without prosthetic group..

A

simple protein