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1A Flashcards

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1
Q

What are carbon containing molecules known as?

A

Organic molecules

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2
Q

What are monosaccharides?

A

The monomers of carbohydrates, e.g. glucose

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3
Q

What is a hexose sugar?

A

A monosaccharide with 6 carbon atoms, e.g. glucose

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4
Q

What are isomers?

A

Molecules with the same molecular formula, however the atoms are connected in a different way. E.g. alpha and beta glucose

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5
Q

Disaccharide formation

A

Two monosaccharides joined together by a condensation reaction, to form a glycosidic bond - water is released

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6
Q

What are polymers?

A

Large, complex molecules composed of a long chain of monomers.

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7
Q

What are monomers?

A

Monomers are small, basic molecular units, e.g. amino acids, monosaccharides and nucleotides

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8
Q

What are Covalent bonds

A

Atoms sharing a pair of electrons on their outer shell. They are strong bonds that require a large amount of energy to break

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9
Q

What are Ionic Bonds

A

Bonds formed between ions - positive ions are attracted to negative ions - ELECTROSTATIC ATTRACTION - they’re weaker than covalent bonds.

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10
Q

Alpha Glucose (Isomer) structure

A

DOWN, DOWN, UP, DOWN (OH groups)

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11
Q

Beta Glucose (Isomer) structure

A

UP, DOWN, UP, DOWN (OH groups)

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12
Q

Disaccharide break down

A

It can be broken down into its monosaccharides by Hydrolysis, a molecule of water is added

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13
Q

Glucose + Glucose =

A

Maltose + water

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14
Q

Glucose + Galactose =

A

Lactose + water

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15
Q

Glucose + Fructose =

A

Sucrose + water

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16
Q

The Benedict’s test for reducing sugars

A

A sample is heated with Benedict’s solution (Blue) A colour change from blue to brick red means reducing sugars are present in the sample. However, it is a semi-quanititive test, as the colour change depends on how much sugar is present, the closer to red, the more sugar; this allows comparing samples. A precipitate is also formed

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17
Q

The Benedict’s test for Non-Reducing sugars

A

if the results for reducing sugars is negative, the solution can be hydrolysed by heating it with dilute hydrochloric acid. Neutralise this with Sodium Hydroxide and test the sample again with Benedict’s solution. If sugars are present, the same colour change of blue to brick red will occur

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18
Q

Biuret Test

A

Testing for protein present. Sodium hydroxide is added to the sample. A few drops of dilute copper sulphate is also added. If a colour change from pale blue to lilac occurs, protein is present in the sample.

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19
Q

Emulsion Test

A

Testing for lipids. The sample is shaken with Ethanol. The sample is then added into water in a test tube. If a milky white precipitate is formed

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20
Q

Iodine Test

A

Testing for Starch. Iodine is dissolved in potassium iodide solution. This solution is added to the sample, and if a colour change from browny-orange to blue-black occurs, starch is present

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21
Q

Types of Starch

A

Amylose and Amylopectin

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22
Q

Structure of Amylose

A

Forms a helical/coiled shape with no branching with alpha Glucose, this means it is more compact in the cell, with only two ends for slow release energy. the structure is held with hydrogen bonds. Present in Plants

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23
Q

Is starch insoluble?

A

Relatively insoluble as both relatively large molecules. Therefore, it doesn’t affect osmosis and water is not drawn into/out of cells.

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24
Q

Structure of Amylopectin

A

Highly branched chain of alpha glucose. its branches allow more enzymes to break down the molecule to get a fast release of energy. Present in Plants

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25
Structure of Glycogen
Animals store excess Glucose as Glycogen. Glycogen is relatively compact but its more highly branched than Amylopectin with Alpha Glucose. As its highly branched, more glucose can be released quickly. It is relatively insoluble, therefore doesn't affect osmosis in cells
26
Structure of Cellulose
Made from long, straight, unbranched chains of Beta Glucose. They run parallel to each other, with hydrogen bonds forming between adjacent chains, to bind them into string MICROFIBRILS. The large number of hydrogen bonds give them strength for providing structural support to plant cells
27
What is it called when pressure of water inside plant cells is at its maximum
Turgid
28
Importance of cellulose in plant cells
Provides rigidity to the plant cell. the strength of cellulose prevents the cell from bursting when water enters by osmosis.
29
What do Lipids contain?
Carbon, Hydrogen and Oxygen
30
When are lipids soluble?
To organic solvents, such as alcohols
31
What are Hydrocarbons? Where are they found?
Hydrocarbons (Molecules that only contain carbon and hydrogen atoms) are present as the Fatty Acid
32
Two Types of Fatty Acids
Saturated - no double bonds present 'saturated' with Hydrogen (Solid at room temperature) Unsaturated - double carbon-carbon bonds, causing a kink in the fatty acid chain. therefore they cannot pack together, making them liquid at room temperature (Oils) - One double carbon-carbon bond is Mono-Unsaturated - More than one double carbon-carbon bond is poly-Unsaturated
33
Two Types of Lipids
Triglycerides and Phospholipids
34
Triglyceride Structure
One molecule of Glycerol joined with Three Fatty Acids with ESTER BONDS by CONDENSATION REACTIONS. The Tails are Hydrophobic, water hating.
35
Phospholipids
A Glycerol molecule with two Fatty Acid chains, and a Phosphate group. They have a hydrophobic tail which repels water, while the Phosphate group 'head' is hydrophilic, attracted to water. Due to 2 ends behaving differently, they are polar.
36
Properties of Triglycerides
Mainly used as energy storage, as the hydrocarbon tails contain lots of chemical energy, which is released when broken down. They're also insoluble to water, so don't affect water potential in cells.
37
Properties of Phospholipids
They make up the Phospholipid Bilayer of cell membranes, controlling what enters and leaves the cell. They form a double layer, with the 'heads' facing out, towards water, whilst the centre of the bilayer is hydrophobic, so water-soluble substances can't easily pass through it.
38
What are Proteins made of?
Monomers of proteins are Amino Acids. A Dipeptide is formed when two Amino Acids are formed. A Polypeptide is formed when more than two Amino Acids join together by Peptide bonds.
39
Amino acid structure
A Carboxyl Group (COOH) and an Amine Group (NH2) as well as an R group attached to a carbon atom. There are only 20 naturally produced amino acids, the only difference is what makes up their R group.
40
Dipeptide and Polypeptide formation
Amino Acids are linked together by a Condensation reaction - A water molecule is released during this reaction. The reverse reaction (Hydrolysis) happens when Dipeptide and Polypeptides are broken down (Using a water molecule(s))
41
Proteins are used in...
Enzymes, Receptors, Antibodies, Carrier and channels in the plasma membranes surrounding cells or structural support - collagen.
42
Protein Structure - Primary
The sequence of Amino Acids in a polypeptide chain
43
Protein Structure- Secondary
The Polypeptide chain is folded into Alpha Helixes and/or Beta sheets by hydrogen bonds
44
Protein Structure - Tertiary
The protein can be twisted and folded into a more complex unique 3D structure, with: - Disulphide bonds - Covalent bonds with amino acids with sulphur present - Ionic Bonds - attraction between negative and positive charges - can be broken by a change in pH - Hydrogen bonds - weak but numerous
45
Protein structure- Quaternary
Multiple Polypeptide chains are linked together, forming large proteins, giving its final 3D structure
46
Enzymes Action
They are globular proteins that act as biological catalysts, catalysing metabolic reactions by lowering the activation energy required to start a chemical reaction. They obtain an active site, which then forms a enzyme-substrate complex (E-S-C) when a substrate, with a complementary shape to the active site of a SPECIFIC ENZYME, is bound
47
How do Enzymes lower the Activation energy?
They Either: - if two substrate molecules need to be joined, being attached to an enzyme holds them close together, reducing any repulsion so they can bond more easily - When the substrate is bound to an active site, it puts a strain on the substrates bonds, so it breaks up more easily
48
The Lock and Key Model for Enzymes
A substrate, with a complementary shape to a specific enzyme and its active site, binds, forming a E-S-C. Any products then leave the active site. the Enzyme molecule is unchanged, and is ready to bind with another substrate molecule
49
The Induced Fit Model for Enzymes
The Active site is not completely complementary to the substrate, however it moulds around the substrate, forming an E-S-C. This model is a better explanation as when the enzyme moulds around the substrate, this puts a strain on the substrates bonds, causing a distortion, reducing the Activation Energy
50
Enzyme Properties
Enzymes properties is related to their Tertiary structure, they are very specific, as their active site is determined by their tertiary structure, so if the substrate isn't complementary to the Active site, an E-S-C won't be formed. If the Tertiary structure is altered in a any way it is denatured, as the substrates cannot fit into the Active site, so the enzyme cannot carry out its function. it may be altered by high temperatures or change in pH
51
Measuring Enzyme Activity
- How Fast the Product is made - measuring the amount of end product at different times during the experiment can calculate the rate of reaction - How fast the Substrate is broken down - measuring the amount of substrate left during different times of the experiment, the rate of reaction can be calculated
52
Enzymes rate of reaction and Temperature increase
- Increases kinetic energy of substrates and enzymes - molecules then move faster and collide more frequently - forming more E-S-C's - Rate of reaction increased. if the temperature is raised too high, the Hydrogen bonds within the Enzymes Tertiary Structure will change, changing the Active sites so the substrate no longer fits, denaturing the enzyme as no E-S-C's can be made. However, different organisms are adapted to different environments and temperatures
53
Enzymes rate of reaction and pH
Most organisms have an optimum pH value. Above or below the pH optimum, number of hydrogen ions and hydroxyl ions change, affecting the charge on the amino acids that make up the Enzyme. Therefore the Ionic and Hydrogen bonds of the enzymes tertiary structure are disrupted and changes, preventing any E-S-C's as the active site would change, denaturing the enzyme.
54
Enzymes rate of reaction and Substrate concentration
Increasing the substrate concentration will increase the rate of reaction as it increases the chance of collision between the active site and substrate. This rate becomes constant at the SATURATION POINT when all the Active sites are occupied, and the substrate concentration is no longer the limiting factor, the enzyme concentration is.
55
Enzyme rate of reaction and Enzyme Concentration
Just like the Substrate concentration, the Enzyme concentration being increased will increase the amount of Active sites available for the substrates to bind and form E-S-C's. This rate then becomes constant at the saturation point, as there isn't enough substrate molecules, and the enzyme concentration is no longer the limiting factor, the substrate concentration is
56
Enzyme Inhibitors - Competitive
Competitive inhibitors are shaped similarly to the substrate molecules and they compete with the Active site of the enzymes. They block the active site from the substrate molecules, stopping E-S-C's, thus slowing the rate of reaction. Higher concentrations of inhibitor, the slower the rate of reaction
57
Enzyme Inhibitors - Non-Competitive
Instead of binding and blocking Active Sites, they bind to part of the enzyme (ALLOSTERIC SITE) this changes the tertiary structure of the enzyme, thus changing the active site, denaturing the enzyme - This is irreversible
58
Measuring the rate of Enzyme-Controlled Reaction
Enzyme Amylase catalyses the break down of starch to Maltose. - Put a drop of iodine solution in each well of a spotting tile - Mix together a known concentration of Starch and Amylase - Using a pipette, drop a bit of the solution into a well at regular intervals until the solution goes browny-orange from blue-black. - You can see how fast the amylase is working by recording how long it takes for the iodine to change colour when the mixture is added. repeat the experiment at different conc.'s and the conc. is repeated at least three times
59
Variables in experimenting the rate of enzyme-controlled Reactions
You can alter these experiments to investigate the effect of different variables, such as pH (adding a buffer solution with different pH to each test tube) or substrate concentration (using serial dilutions) Remember: only change one variable, everything else must stay the same!
60
Estimating the initial rate of reaction
Using a Tangent Line on a graph from Time=0, using a ruler. Then draw a line with the ruler where the line would have continued if it carried on as 0. - Calculate the gradient of the tangent - change in Y axis / Change in X axis - change the units - divide the y axis units by the x axis units

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