C1 Biological Molecules Flashcards

(46 cards)

1
Q

Condensation reaction

A

A reaction in which water molecules are formed when monomers are joined together

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2
Q

Hydrolysis

A

(Inverse of condensation reaction) - Adding water to a polymer to split it

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3
Q

Polymer

A

Large molecules made by bonding single repeating units

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4
Q

Monomer

A

Repeating unit that joins to form polymers

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5
Q

Disacchardies

A

Formed when monosaccharides join via a condensation reaction with glycosidic bonds in between

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6
Q

Glycosidic Bonds

A

Bonds between monosaccharides in a di/polysaccharide

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7
Q

Types of Monosaccharides

A

Fructose, Galactose, Glucose

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8
Q

Types of Disaccharides

A

Sucrose, Lactose, Maltose

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9
Q

Glucose + Fructose

A

Sucrose

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10
Q

Galactose + Glucose

A

Lactose

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11
Q

Glucose + Glucose

A

Maltose

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12
Q

Reducing sugar

A

Sugars that acts as a reducing agent in chemical reactions (donate electrons to other molecules)

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13
Q

Non - reducing sugar

A

Does not donate electrons

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14
Q

Test for REDUCING sugar

A

Benedict’s;
1. Benedict’s solution in a tube with water
2. Grind the solution with mortar and pestle and distilled water
3. Put the sample in a test tube
4. Heat with a water bath
5. If positive, the solution with turn BRICK RED (from blue)

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15
Q

Test for NON-REDUCING sugars

A

If negative for reducing sugars:
1. Add dilute HCl
2. Add sodium carbonate to neutralise
3. Add Benedict’s solution & gently heat

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16
Q

Polysaccharides

A

A molecule made up of more than 2 monosaccharides

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17
Q

Types of Polysaccharides

A

Starch, Glycogen, Cellulose

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18
Q

Properties of Starch

A
  1. Insoluble; doesn’t affect water potential (water isn’t drawn into the cell via osmosis
  2. Large; doesn’t diffuse out of cells
  3. Compact; can fit large amounts into small spaces
  4. Breaks down into alpha glucose when hydrolysed; stored in small spaces & transported to be ready for use in respiration
  5. Branched form (many ends); each can have an enzyme attached to the end to be acted on rapidly to release glucose - (1,4) & (1,6) bonds; more branches
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19
Q

Properties of Glycogen

A
  • Insoluble; doesn’t affect water potential (water isn’t drawn into the cell via osmosis
  • Large; doesn’t diffuse out of cells
  • Compact; can fit large amounts into small spaces
  • MORE branched than starch; more enzymes > more rapid release of glucose for respiration (animals have higher metabolic rates than plants (starch))
  • (1,4) & (1,6) bonds; more branches
20
Q

Properties of Cellulose

A
  • made of BETA glucose; forms long straight unbranched chains
  • chain run parallel + CROSSLINK via H BONDS; making the structure stronger
  • molecules are grouped to form MICROFIBRES which then group to form FIBRES; which adds to the strength of the polymer
21
Q

Triglyceride

A

3 fatty acids with ester bonds between glycerol (hence glyceride)

22
Q

Saturated

A

Fatty acid with no carbon-carbon double bond; bonded to max number of hydrogen atoms (monounsaturated if 1 double bond)

23
Q

Unsaturated

A

Fatty acid with carbon-carbon double bond; bonded to max number of hydrogen atoms (polyunsaturated if multiple double bond)

24
Q

Phospholipid

A

Similar to triglyceride
- 2 fatty acids instead of 3; one replaced by a phosphate molecule

25
Phospholipid structure
-Have 2 parts: -Hydrophilic 'head' > attracted to water -Hydrophobic tail > orients away from water -2 ends are POLAR (behave differently) -when placed in water, they orient themselves so that the hydrophilic head is closer to the water
26
Roles of lipids
1. Cell membrane - flexibility of membrane 2. Source of Energy - releases more than 2x the energy the same mass of carbohydrates do when oxidised 3. Waterproofing - insoluble in water = waterproofing eg: plants w/ waxy cuticles, mammals w/ oily secretion from sebaceous glands in the skin 4. Insulation - slow conductors of heat; help retain heat when stored beneath body surface 5. Protection - fat is stored around the delicate organs
27
Polypeptide
molecule made up of MORE THAN 2 amino acids
28
Peptide bond
Bond betweeen the 2 amino acids
29
Primary Structure
Peptide bonds between amino acids
30
Secondary Structure
- Alpha = helix - Beta = pleated sheet; with H bonds between amino group H+ and Carboxyl group H
31
Tertiary Structure
-H bonds -Disulfide bridges, and ionic bonds between R groups(makes it into a globular protein)
32
Quaternary Structure
Consists of many different polypeptides
33
Activation energy
The minimum amount of energy required for a reaction to take place
34
Active site
The area of the enzyme where the reaction with the substrate takes place
35
Substrate
The chemical reactant that enzymes bind to
36
Induced Fit Model
The idea that the active site of the enzyme changes shape slightly due to bonds distorting as the substrate binds to it to better fit the shape of the active site
37
Competitive Inhibitors
Compete with the substrate for the active site > binds to the active site to prevent the substrate
38
Non-competitive Inhibitors
Binds to a different site on the enzyme, changing the shape of the enzyme preventing the enzyme from binding to the substrate effectively
39
Factors affecting enzyme activity
-Temperature; when the temp gets too high, H bonds & others begin to break in the enzyme, therefore enzyme (and its active site with it) changes shape (DENATURATION) -pH; changes the charge on the amino acid that makes up the active site, causes the bonds maintaining the tertiary structure to break, changing the shape of the active site -Enzyme concentration
40
LOW enzyme concentration
Too few enzymes to allow substrates to be broken down
41
What will the rate of reaction be like with an INTERMEDIATE enzyme concentration?
DOUBLES as there are enough enzymes for the substrates
42
Inorganic ions
Sodium, Phosphate, Hydrogen, Iron
43
Sodium ions
Involved in nerve impulse transmission, the control of cell osmotic pressure and the absorption of molecules such as glucose into the cell. Actively transported outside of a cell across the plasma membrane using ATP. As it is now at a higher concentration gradient outside of the cell, it diffuses back in via a channel protein, along with a glucose molecule against the concentration gradient. Ensures that all available glucose produced during digestion is utilised.
44
Phosphate Ions
Phosphorus is chemically bonded to other atoms, in this case, 3 oxygen atoms. Forms the phosphodiester backbone of DNA and RNA. In ATP 3 phosphate ions are linked to ribose and Adenine. These bonds are unstable and, therefore only require a small amount of activation energy which releases a lot of energy.
45
Hydrogen ions
Responsible for the pH of a cell. This is a critical role as a significant change would result in the denaturation of enzymes in the cytoplasm. In reality, the pH fluctuations are only slight, which would more likely affect the activity of the enzyme. Hydrogen results in a buffering effect of haemoglobin. During the transport of carbon dioxide, it forms hydrogen carbonate in the blood.
46
Iron ions
Involved in the transport of oxygen. They form the prosthetic group, haem. There are 4 haem groups per haemoglobin molecule which can reversibly bind molecules of oxygen each.