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Biological Molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What is the test for reducing sugars?

A
  1. Add the food sample make sure it is in liquid form
  2. Add equal volume of Benedict’s
  3. Heat the mixture
  4. If sugar present then goes from blue to orange, red
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2
Q

What is the definition of a monomer?

A

Smaller units from which larger molecules are made

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3
Q

What is the definition of a polymer?

A

Large number of monomers joined together

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4
Q

What is a condensation reaction?

A

Joining of two molecules with the formation of a chemical bond and involves the elimination of a water molecule

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5
Q

What is a hydrolysis reaction?

A

Breaks a chemical bond between two molecules and involves the use of a water molecule

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6
Q

What two monosaccharides make maltose?

A

Two alpha glucose molecules

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7
Q

What two monosaccharides make sucrose?

A

Alpha glucose molecule and a fructose molecule

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8
Q

What two monosaccharides make lactose

A

A glucose molecule and a fructose molecule

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9
Q

What is the structure of a-glucose and B-glucose?

A

A-glucose OH group on the bottom
B-glucose OH group on the top

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10
Q

What is the test for non reducing sugars?

A
  1. Sample in liquid form
  2. Add Benedict’s reagent
  3. Place in boiling water no colour change reducing sugar not present
  4. Ass new food sample add HCl and boil hydrolyses disaccharide
  5. Add sodium hydrogencarbonate
  6. Heat with Benedict’s
  7. If present turns an orange brown
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11
Q

What is the test for starch?

A
  1. Add food sample
  2. Add iodine
  3. Turns blue-black
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12
Q

What are the features of starch?

A
  1. Insoluble
  2. Does not diffuse out of cells
  3. Compact lots in small space
  4. A-glucose used in respiration
  5. Many ends so enzymes can act on it
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13
Q

What are the features of cellulose?

A
  1. Straight un branched chains
  2. Collective strength of hydrogen bonds
  3. Provides strength to the cell wall
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14
Q

What are the features of glycogen?

A
  1. Insoluble
  2. Does not diffuse out of cells
  3. Compact lots stored in small space
  4. Highly branched can be acted on by enzymes
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15
Q

How are triglycerides formed?

A

A condensation reaction of one glycerol molecule and 3 fatty acids. This forms an ester bond

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16
Q

What is the structure of a phospholipid ?

A

One glycerol, 2 fatty acids and a phosphate group.

17
Q

What are the properties of triglycerides?

A
  1. High ratio of energy storing carbon hydrogen bonds so good source of energy
  2. Low mass to energy ratio good storage molecule good for animals less mass to carry
  3. Large non polar so insoluble
  4. Release water when oxidised
18
Q

What are the properties of phospholipids?

A
  1. Polar molecules hydrophilic head and hydrophobic tail this means that they can form a bilayer and a hydrophobic barrier between the inside and outside of the cell
  2. Can form glycolipids which are important in cell recognition
19
Q

What is the test for lipids?

A
  1. Add the sample
  2. Add the ethanol
  3. Shake and then add the water
  4. A milky while emulsion indicates a lipid present
20
Q

What is the general structure of an amino acid?

A

R
|
H2N——C—-COOH
|
H

21
Q

How are dipeptides formed?

A

In a condensation reaction between two amino acids

22
Q

What is a primary structure of a protein?

A

A sequence of amino acids in a polypeptide chain

23
Q

What is a secondary structure of a protein?

A

The folding of a polypeptide creating more hydrogen bonds can be hydrogen bonds and B pleated sheets

24
Q

What is the tertiary structure of a protein?

A

Further coiling and folding includes ionic, disulphide and hydrogen bonds

25
Q

What is the quaternary structure of a protein?

A

Different polypeptide chains associated with prosthetic groups into large complex molecules

26
Q

What is the test for proteins?

A
  1. Place a sample of the solution and add biuret reagent
  2. If the solution turns purple there is a peptide bond present if there is no protein remains blue
27
Q

What is the role of an enzyme?

A

Lowers the activation energy for the reaction it catalyses

28
Q

Describe the induced fit model for an enzyme?

A

When a substrate is present the enzyme is induced to change shape at the active site and to fit together with the substrate
The enzyme and the substrate join to form an enzyme substrate complex the enzyme does its job and the products are released

29
Q

Explain the effect that temperature has on an enzyme?

A
  1. Kinetic energy increases so more molecules collide with each other resulting in more enzyme substrate complex’s
  2. The temperature rise breaks hydrogen bonds causing the active site to change shape which slows the rate of reaction
  3. Eventually the enzyme will denature so the enzyme does not function again causing a falling line
  4. Enzymes have an optimum temperature the enzymes work at
30
Q

What effect does PH have on an enzyme?

A
  1. The change in PH alters the charges on the amino acids at the active site so the substrate can no longer bind
  2. This may cause the bonds in the tertiary structure to break so the active site changes shape
  3. pH changes more likely to reduce enzyme activity
31
Q

What is the effect on enzyme concentration on rate of reaction?

A
  1. At low enzyme concentrations there are few enzymes to allow all substrate molecules to have an active site
  2. Balanced concentration all substrate molecules can occupy an active site
  3. High enzyme concentrations have no effect as there is enough active sites to occupy the substrate
32
Q

What is the effect of substrate concentration on rate of reaction?

A
  1. At low concentration few molecules can occupy the active site
  2. At balanced all the active sites can be occupied
  3. High substrate concentration has no effect because there is not enough active sites
33
Q

What effect do competitive inhibitors have?

A
  1. They have a similar shape to the substrate so they can occupy the active site
  2. If substrate concentrations are increased there is a reduced effect on the inhibitor
  3. When the inhibitor leaves there can be another molecule that can bind to the active site
34
Q

What effect do non-competitive inhibitors have?

A
  1. They attach a an allosteric site this alters the shape of the active site
  2. An increase in substrate concentration has no effect on the inhibitor

Biology (20 decks)

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