Biological molecules Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

What are the functions of water?

A
  • Water is a reactant in lots of important chemical reactions, including hydrolysis reactions.
  • Water is a solvent, and most biological reactions take place in solution so water is really essential.
  • Water also transports substances. Because it is a liquid and a solvent it can easily transport lots of materials like glucose and oxygen around plants and animal cells.
  • Water helps with temperature control as it has a high specific heat capacity and a high latent heat of evaporation.
  • Water is a habitat due to its qualities of temperature regulation- meaning lots of organisms can survive and reproduce in it.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What is the structure of a water molecule?

A

A molecule of water is made up of two hydrogen atoms and an oxygen atom, held together by a shared pair of electrons/covalent bonds.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Why are water molecules dipolar?

A

Because the shared pair of electrons are pulled closer to the oxygen atom- due to a greater positive attraction- the oxygen atom becomes slightly negative and therefore the hydrogen atom becomes slightly positive. This slight charge on either atom makes it a polar molecule.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

How do hydrogen bonds in water work?

A

The slightly negatively charged oxygen atoms attract the slightly positively charged hydrogen atoms of other water molecules.
This attraction is called hydrogen bonding and it gives water some of its useful properties.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

How do hydrogen bonds give water a high specific heat capacity?

A

Specific heat capacity is the temperature required to raise 1 gram of a substance by 1 degree C. The hydrogen bonds between the water molecules can absorb a lot of energy. So water has a high heat capacity as it takes a lot of energy to heat up.
This means that water doesn’t experience rapid temperature changes making it a stable environment/habitat for organisms to live in.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

How do hydrogen bonds give water a high latent heat of evaporation?

A

It takes a lot of heat energy to break the many hydrogen bonds in water so water has a high latent heat of evaporation as it takes a lot of energy to evaporate. This is useful in living organisms for cooling things- like sweat taking lots of heat away when it evaporates and thus cools us down.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

How does water’s polarity make it very cohesive?

A

Cohesion is the attraction between molecules of the same type, water molecules are very cohesive because they are polar.
This helps water to flow, making it great for transporting substances. It also helps water to be transported up plant stems in the transpiration stream.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

How does water’s polarity help to make it a good solvent?

A

A lot of important substances in biological reactions are ionic, meaning they are made up of one positive atom/molecule and a negative atom/molecule. Because the water is polar, the slightly positive end will be attracted to the negatively charged ions, and the negative end to the positively charged ions. This means the ions will be surrounded by water molecules/they’ll dissolve.
This is useful as ions can be dissolved in the water in the blood and then carried around the body.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Why is the fact that water’s less dense when it’s solid useful?

A

As temperature drops water cools down and turns from a liquid to a solid. Water molecules are held further apart in ice than in liquid water because each water molecule forms four hydrogen bonds with other water molecules- making a lattice shape. This makes ice less dense than water, which is why it floats.
This is useful in living organisms because in cold temperatures ice forms an insulating layer on top of the water and the water underneath doesn’t freeze and remains at a nice temperature and fish can still move around.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What are Carbohydrates?

A

Carbohydrates are polymers, polymers are molecules made up of many different smaller molecules called monomers bonded together. The monomers that make-up carbohydrates are called monosaccharides.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What kind of monosaccharide is glucose?

A

Glucose is a hexose sugar as it contains six carbon atoms.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What are the two structures of glucose?

A

There are two forms of glucose; alpha and beta glucose. They both form ring structures.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

How is glucose’s structure related to its function?

A

It’s the main energy source in plants and animals so, its structure makes it soluble so it can be easily transported. Its chemical bonds also contain lots of energy.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What is ribose’s structure and function?

A

Ribose is a monosaccharide with five carbon atoms, meaning it is a pentose sugar. Its structure is: CH2OH-CH-CHOH-CHOH-CHOH-O- (back to CH)
It is the sugar component of RNA nucleotides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What are the bonds that monosaccharides form when bonded together?

A

A glycosidic bond (1,4 in glucose)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What is a condensation reaction (in polymerization)?

A

A hydrogen atom on one monosaccharide bonds to a hydroxyl group on the other, releasing a molecule of water.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What elements are all carbohydrates made up of?

A

Carbon, Hydrogen, and Oxygen. The ratio is usually CnH2nOn

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What is a hydrolysis reaction (in polymerization)?

A

A molecule of water reacts with the glycosidic bond, breaking it apart.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

How are disaccharides formed?

A

Disaccharides are formed when two monosaccharides join together,
maltose = glucose (A) + glucose (A)
sucrose = glucose (A) + fructose
lactose = glucose (A or B) + galactose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

How are polysaccharides formed?

A

A polysaccharide is formed when more than two monosaccharides join together. For example, lots of glucose (A) join together to form amylose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

What is the structure of starch?

A
  • Starch is a mixture of two polysaccharides of alpha-glucose (amylose and amylopectin)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

What is the function of starch?

A
  • Plants store excess glucose as starch and use it as a store it can break down to get glucose when it is needed (because glucose is soluble and starch is not, it doesn’t mess with the water potential of the cell and cause osmosis.)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

What is the structure and function of amylose?

A

Amylose is a long branch chain of alpha-glucose. The angles of the glycosidic bond give it a coiled structure. This makes it compact, so it’s really good for storage because you can fit more into a smaller space.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

What is the structure and function of amylopectin?

A

It’s a long, branched chain of alpha glucose. Its side branches allow the enzymes to break down the molecule to get at the glycosidic bonds easily. This means that the glucose can be released quickly.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

What is the structure of glycogen?

A

Glycogen is a polysaccharide of alpha glucose and its structure is very similar to amylopectin. However, it has more side branches coming off of it. Lots of branches mean that stored glucose can be released quickly, which is important for energy release in animals. It is also very compact, which means it is good for storage

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

What is the function of glycogen?

A

Animal cells get energy from glucose too. But animals choose to store excess glucose as glycogen- as it is insoluble.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

What is the structure of cellulose?

A

Cellulose is made up of long unbranching chains of beta glucose. When beta-glucose molecules form they form straight-chain molecules. The cellulose chains are linked together by hydrogen bonds to form strong fibers called microfibrils.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

What is the function of cellulose?

A

Cellulose provides structural support for cells (i.e. in plant cell walls)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

What are triglycerides?

A

Triglycerides are macromolecules (complex molecules with a large molecular mass), as with all lipids they contain Carbon, Hydrogen, and Oxygen. They are composed of one molecule of glycerol with three fatty acid tails attached to them.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

What is the structure of a triglyceride?

A

They are composed of one molecule of glycerol with three fatty acid tails attached to them. The fatty acid molecules have long tails made of hydrocarbons. The tails are hydrophobic, which means lipids are insoluble in water. All fatty acids have the same basic structure, but the hydrocarbon tail varies.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

How are triglycerides and ester bonds related?

A

Triglycerides are synthesized by the formation of an ester bond between each fatty acid and the glycerol molecule. The ester bonds are formed by a condensation reaction. This is called esterification. Hydrolysis can reverse the ester bonds- breaking down the triglyceride using water.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

What are the differences between saturated and unsaturated fatty acids?

A

Saturated fatty acids don’t have any double bonds between carbon atoms. Unsaturated fatty acids have at least one double bond between carbon atoms. Mono-unsaturated means one and poly-unsaturated means more than one.
(having a double bond causes the chain to kink- the more you have, the less straight the chain)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

How are phospholipids similar to triglycerides?

A

Phospholipids are macromolecules. They’re pretty similar to triglycerides except one of the fatty acid molecules is replaced by a phosphate group. The phosphate group is hydrophilic while the fatty acid tails are hydrophobic.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

How is the structure of Triglycerides related to their function?

A

They are used mainly as storage molecules in animals and plants, but some bacteria use them to store energy and carbon.
- The long hydrocarbon chains of the fatty acids contain lots of chemical energy which is released when they’re broken down. Because of this lipids contain twice as much energy/g as carbohydrates.
- They’re insoluble so they don’t cause water to enter the cell via osmosis. They bundle together as insoluble droplets due to the hydrophobic tails bundling together using their glycerol heads to shield themselves.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

How is the structure of phospholipids related to their function?

A

Phospholipids are found in the cell membranes of all eukaryotes and prokaryotes. They make up the phospholipid bilayer which controls what substances can enter and leave a cell.
- Phospholipid heads are hydrophilic and their tails are hydrophobic. so they form a double layer with their heads facing out towards the water on either side
- The center of the bilayer is hydrophobic so water-soluble substances like ions can’t easily pass through it- the membrane acts as a barrier to those substances.

36
Q

How is the structure of cholesterol related to its function?

A

Cholesterol is a type of lipid with a hydrocarbon ring structure attached to a hydrocarbon cell. The ring has a polar hydroxyl group attached to it. In eukaryotic cells, cholesterol helps to regulate the fluidity of the cell membrane by interacting with the phospholipid bilayer.
- It has a small size and flattened shape, meaning it can fit in between the phospholipid molecules in the bilayer
- At higher temperatures, they bind to the hydrophobic tails of the phospholipids and cause them to pack closer together. This makes the membrane less fluid and more rigid. ( the reverse happens at colder temperatures)

37
Q

What is the structure of proteins (levels)?

A
  • They are polymers
  • Amino acids are the monomers in proteins
  • A dipeptide is formed when two amino acids join together
  • A polypeptide is formed when more than two amino acids are joined together
  • Proteins are made up of one or more polypeptides
38
Q

What is the structure of amino acids?

A

All amino acids have the same general structure: a carboxyl group and an amino group attached to a carbon atom. What makes them different is the variable group they contain.
All amino acids contain Carbon, Hydrogen, Oxygen, and Nitrogen and some also contain sulfur.

39
Q

How are amino acids joined together?

A

Amino acids are joined together by peptide bonds to form dipeptides and polypeptides. A molecule of water is released during this reaction- meaning it is a condensation reaction. A hydrolysis reaction can be used to break the bonds.

40
Q

What is a protein’s Primary structure?

A

The primary structure is the sequence of amino acids in the polypeptide chain. Different structures have different sequences of amino acids in their primary structure. A change in one amino acid may change the structure of a whole protein.

41
Q

What is a protein’s Secondary structure?

A

The polypeptide chain doesn’t remain flat and straight. Hydrogen bonds form between nearby amino acids in the chain. This makes it automatically coil into an alpha helix or fold into a beta pleated sheet- this is the secondary structure.

42
Q

What is a protein’s Tertiary structure?

A

The coiled or folded chains of amino acids are often coiled and folded further. More bonds form between different parts of the polypeptide chain. For proteins made from a single polypeptide chain, the tertiary structure forms their final 3D structure.

43
Q

What is a protein’s Quaternary structure?

A

Some proteins are made of several different polypeptide chains held together by bonds. The quaternary structure is the way these polypeptide chains are assembled together. For proteins made of four polypeptide chains, bonded together. For proteins made from more than one polypeptide chain, the quaternary structure is the protein’s final 3D structure.

44
Q

How can we get 3D models of proteins?

A

Computer modelling can create 3D interactive images of proteins which makes it really useful for investigating the different levels of structure in a protein molecule.

45
Q

What are the bonds in the primary level of a protein?

A

Held together by the peptide bonds between amino acids.

46
Q

What are the bonds in the secondary level of a protein?

A

Held together by hydrogen bonds.

47
Q

What are the bonds in the tertiary level of a protein?

A

Held together by
- ionic bonds (neg R groups attracted to pos R groups)
- disulfide bonds (when two molecules of the amino acid cysteine come close the sulfur atom in one bonds to the other)
- hydrophobic and hydrophilic interactions ( when hydrophobic R groups are close together they tend to clump, so hydrophilic R groups are more likely to be pushed to the outside- affecting their final structure when folded)
- hydrogen bonds ( weak bonds formed between slightpos H atoms in one R group and slightneg atoms in other R groups)

48
Q

What are the bonds in the quaternary level of the protein?

A

This tends to be determined by the bonds in the tertiary structure.

49
Q

Why are globular proteins soluble?

A

Inside a globular protein, the hydrophilic R groups on the amino acid tend to be pushed to the outside of the molecule. This is caused by the hydrophobic and hydrophilic interactions in the protein’s tertiary structure. This makes globular proteins soluble, so they are easily transported in fluids.

50
Q

What are the functions of globular proteins in living organisms (Haemoglobin)?

A

Haemoglobin is a globular protein that carries oxygen around the body in red blood cells. It is a conjugated protein. Each of the four polypeptide chains in hemoglobin has a prosthetic group called haem. A haem group contains iron, which oxygen binds to.

51
Q

What are the functions of globular proteins in living organisms (Insulin)?

A

Insulin is a hormone secreted by the pancreas. It helps to regulate the blood glucose level. Its solubility is important because it means it can be transported in the blood to the tissues where it acts. An insulin molecule consists of two polypeptide chains, which are held together by disulfide bonds.

52
Q

What are the functions of globular proteins in living organisms (Amylase)?

A

Amylase is an enzyme that catalyzes the breakdown of starch in the digestive system. It is made up of a single chain of amino acids. Its secondary structure contains both alpha helix and beta pleated sheet sections. Most enzymes are globular proteins.

53
Q

What is a conjugated protein?

A

A conjugated protein is a protein with a non-protein group attached. the non-protein part is called a prosthetic group.

54
Q

What are fibrous proteins?

A

Fibrous proteins are insoluble and strong. They’re structural proteins and are fairy unreactive (unlike many globular proteins).

55
Q

What is collagen?

A

Collagen is a type of fibrous protein. It is found in animal connective tissues, such as bone, skin, and muscle. It is a very strong molecule. Minerals can bind to the protein to increase its rigidity, e.g. in bone.

56
Q

What is keratin?

A

Keratin is a type of fibrous protein. It is found in many of the external structures of animals, such as skin, hair, nails, feathers, and horns. It can either be flexible (as it is in skin) or hard and tough (as it is in nails).

57
Q

What is Elastin?

A

Elastin is a type of fibrous protein. It is found in elastic connective tissue, such as skin, large blood vessels, and some ligaments. It is elastic, so it allows tissues to return to their original shape after they have been stretched.

58
Q

What are ions and inorganic ions?

A

Ions are atoms/groups of atoms with an electric charge
Negatively charged ions are called anions, and Positively charged ions are called cations.
An inorganic ion is one which doesn’t contain carbon (although there are exceptions). Inorganic ions are really important to biological processes.

59
Q

What is the function of calcium ions in biological processes?

A
  • They are involved in the transmission of nerve impulses and the release of insulin from the pancreas.
  • They also act as a cofactor for many enzymes.
  • They are also important for bone formation.
60
Q

What is the function of sodium ions in biological processes?

A
  • They are important for generating nerve impulses, muscle contraction, and regulating fluid balance in the body.
61
Q

What is the function of potassium ions in biological processes?

A
  • They are important for generating nerve impulses, muscle contraction, and regulating fluid balance in the body.
  • They also activate essential enzymes needed for photosynthesis in plant cells.
62
Q

What is the function of hydrogen ions in biological processes?

A
  • They affect the pH of a solution (more H ions in comparison to OH makes it an acid)
  • They are also important for photosynthesis reactions that occur in the thylakoid membranes inside chloroplasts.
63
Q

What is the function of ammonium ions in biological processes?

A
  • They are absorbed from the soil by plants and are an important source of nitrogen which is used to make amino acids and nucleic acids.
64
Q

What is the function of nitrate ions in biological processes?

A
  • They are absorbed from the soil by plants and are an important source of nitrogen which is used to make amino acids and nucleic acids.
65
Q

What is the function of hydrogencarbonate ions in biological processes?

A
  • They act as a buffer, which helps to maintain the pH of the blood.
66
Q

What is the function of chloride ions in biological processes?

A
  • They are involved in the ‘chloride shift’ which helps to maintain the pH of the blood during gas exchange.
  • They act as a cofactor for the enzyme amylase.
  • They are also involved in some nerve impulses.
67
Q

What is the function of phosphate ions in biological processes?

A
  • They are involved in photosynthesis and respiration reactions.
  • They are needed for the synthesis of many biological molecules like nucleotides, phospholipids, and calcium phosphate.
68
Q

What is the function of hydroxide ions in biological processes?

A
  • They affect the pH of the substances (more OH ions than H ions makes an alkali)
69
Q

What are reducing sugars?

A

Reducing sugars include all monosaccharides (glucose) and some disaccharides (maltose and lactose).

70
Q

How do you test for reducing sugars?

A

1) Add benedicts reagent (blue) to a sample and heat it in a water bath that has been brought to the boil.
2) The color of the precipitate changes from blue-green-yellow-orange-brick red.
3) If the test is positive it will form a coloured precipitate.
4) The higher the concentration of the reducing sugar, the further the color change goes. You can use this to compare the amount of reducing sugars in different solutions. A more accurate way to do this is either using a colorimeter or weighing the precipitate.

71
Q

How do you test for non-reducing sugars?

A

1) If the result of the reducing sugars test is negative, there could still be a non-reducing sugar present. To test for non-reducing sugars like sucrose you need to break them down into monosaccharides.
2) Get a sample of the test solution add dilute HCl and carefully heat in a water bath. Then neutralize it with sodium hydrogencarbonate and repeat the benedicts test.

72
Q

How can you test for glucose using test strips?

A

Dip test strips coated in a reagent into your test solution. It will change colour if glucose is present and you can refer to a colour chart to gain an indication of the concentration of glucose present. The strips are particularly useful for testing a person’s urine for glucose- indicating diabetes.

73
Q

How can you test for Starch using iodine?

A

Add iodine dissolved in potassium iodide solution to the test sample. If starch is present then the sample changes from brown-orange to blue-black. If starch isn’t present it will remain brown-orange.

74
Q

How can you test for proteins using Biuret?

A

1) The test solution needs to be alkaline, so first you add a few drops of sodium hydroxide solution.
2) Then add some copper (II) sulfate solution. If there is protein present it will turn from blue to purple. If no protein is present then it will remain blue.

75
Q

How can you test for lipids using the emulsion test?

A

Shake the test substance with ethanol for about a minute, then pour the solution into water. If lipid is present the solution will turn milky. The more lipid the more noticeable the milky colour will be. If there is no lipid the solution will remain clear.

76
Q

What is a colorimeter and how can it determine the concentration of a glucose solution?

A

You can use Benedict’s reagent and a colorimeter to get a quantitative estimate of how much glucose there is in a solution. A colorimeter is a device that measures the strength of a solution by seeing how much light passes through it. A colorimeter measures absorbance. The more concentrated the solution the greater the absorbance.

77
Q

How do you use a colorimeter to determine the concentration of a glucose solution (serial dilution)?

A

1) Line up five test tubes in a rack
2) add 10cm3 of the glucose solution to the first test tube and 5cm3 of distilled water to the other test tubes.
3) add 5cm3 from the first test tube to the second and mix thoroughly.
4) repeat the process three more times.

78
Q

How do you use a colorimeter to determine the concentration of a glucose solution (Calibration curve)?

A

1)Do a benedicts test on each solution as well as a negative control of pure water. Use the same amount of benedicts in each case.
2) Remove any precipitate (either leave 24 hours and it settles out or centrifuge)
3) Use a colorimeter ( with a red filter) to measure the absorbance of the benedicts solution remaining in each tube.
4) use the results to make a calibration curve showing absorbance against glucose concentration.
you could then figure out an unknown solution in the same way as the known one and use the curve to figure out its concentration.

79
Q

What is a biosensor and how does it work?

A

A biosensor is a device that uses a biological molecule, such as an enzyme to detect a chemical. The biological molecule produces a signal which is converted to an electrical signal by a transducer. The electrical signal is then processed and can be used to work out other information.

80
Q

How do glucose biosensors work?

A

1) A glucose biosensor is used to determine the concentration of glucose in a solution.
2) It does this using the enzyme glucose oxidase and electrodes.
3) The enzyme catalyzes the oxidation of glucose at the electrodes- this creates a charge, which is converted into an electrical signal by the electrodes (the transducer).
4) The electrical signal is then processed to work out the initial glucose concentration.

81
Q

What is chromatography and how is it useful?

A

Chromatography is used to separate stuff in a mixture so that you can identify its components. For example, chromatography can be used to separate and identify biological molecules like amino acids, carbohydrates, vitamins, and nucleic acids.
There are lots of types of chromatography like paper chromatography and thin-layer chromatography.

82
Q

How does chromatography work?

A

1) All types of chromatography have the same basic setup of a mobile phase where the molecules can move (liquid solvents like water and ethanol) and a stationary phase where the molecules can’t move (paper in a paper-thin layer of solid like glass or plastic in a thin layer)
2) They all use the same principles
- the mobile phase moves through or over the stationary phase
- the components of the mixtures spend different amounts of time in each phase
- the components that spend the longest in the mobile move the furthest
- the time spent in different phases is what spreads out the components

83
Q

How do you use paper chromatography to identify amino acids?

A

1) draw a pencil line at the bottom of a piece of chromatography paper and put a concentrated spot of the amino acid mixture on it. (could roll into cylinder now)
2) Add a small amount of prepared solvent (usually a mixture of butan-1-ol, glacial ethanoic acid, and water) to a beaker and dip the bottom of the paper in it. Do it in a fume cupboard and cover it with a lid to stop solvent from evaporating.
3) As the solvent spreads up the paper, the amino acids move (but at different rates)
4) When the solvent has nearly reached the top, take the paper out and mark the solvent front with a pencil. Then leave to dry out.
5) Spray with ninhydrin solution to turn the amino acids purple so you can see them. Do this in a fume cupboard and use gloves, this only works for amino acids and proteins.
6) Then calculate their Rf values and look at a database to see which amino acids are contained in the solution.

84
Q

What is the equation for the Rf value?

A

Distance traveled by solute/Distance traveled by solvent

85
Q

What is the optimum water bath temperature to carry out benedicts test for sugars?

A

around 95 degrees