bio mock Flashcards

1
Q

describe the structure of a triglyceride

A
  • three fatty acid chains attached by a glycerol backbone

- fatty acids- chains of carbon atoms with the end carbon possessing a carboxyl group

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

describe the structure of cellulose

A

polysaccharide
- polymer consisting of long unbranched chains of beta-glucose joined together by 1, 4 glycosidic bonds

-to form the 1, 4 glycosidic bonds every other beta-glucose molecule has to be inverted.

inversion gives strength as many hydrogen bonds form between the long chains, this is important because cellulose is the main structural component of cell walls

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

describe the structure of glucose

and draw an alpha and beta glucose molecule

A
  • glucose is the monomer for carbohydrates

glucose is a monosaccharide and can exist in two different forms (isomers) which are alpha-glucose and beta-glucose

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

describe the structure of starch

A
  • starch is a storage polysaccharide (macromolecule)
  • it is constructed from two different polysaccharides (amylose and amylopectin)

amylose - unbranched helix with 1, 4 glycosidic bonds between alpha glucose molecules (helix shape allows for it to be more compact and more resistant to digestion)

amylopectin - 1,4 glycosidic bonds between alpha glucose molecules but also 1, 6 glycosidic bonds form between glucose molecules creating a branched molecule (branched so glucose molecules can be easily added to for storage

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

describe the structure of glycogen

A
  • storage polysaccharide of animals and fungi
  • highly branched and not coiled
  • more compact then amylopectin
  • branches enable more free ends where glucose molecules can either be added or removed allowing for condensation and hydrolysis reactiosn to occur more rapidly
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

coversions for cm to mm to um to nm

A

cm ——> mm = x10
mm —–> um = x1000
um ——> nm = x1000

DIVIDE FOR REVERSE

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

describe different types of microscopes

A

LIGHT MICROSCOPE

  • uses light to form an image
  • using light makes if impossible to distinguish between two objects that are closer than half the wavelength of light (500-650 / 2)
  • low max resolution
  • can only used to see eukaryotic cells and their nuclei (sometimes chloroplasts and mitochondria

ELECTRON MICROSCOPES

  • uses electrons to form an image
  • electrons have a much smaller wavelength than light, so it can distinguish between two objects that are extremely close together

TRANSMISSION ELECTRON MICROSCOPES

  • beam of electrons transmitted through the specimen
  • denser parts of the specimen absorb more electrons making the denser parts appear darker on the final image
  • gives high res images and allows internal structures to be seen
  • cannot be used to observe live specimens
  • lengthy treatment to prepare specimens which can introduce artefacts
  • do not produce colour image
  • used only with very thin specimens

SCANNING ELECTRON MICROSCOPE

  • uses beam of electrons which bounce off the surface of the specimen, the electrons are detected which form an image
  • this means 3-D images can be produces
  • can be used on thick or 3-d specimens and allow the external, 3-d structure of specimens to be observed
  • give lower res than TEMs
  • cannot be used to observe live specimens
  • do not produce colour image
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

how are peptide bonds formed and broken

draw a diagram of amino acids bonding together

A

peptide bonds are what bond amino acids together

  • a hydroxyl group (OH) is lost from a carboxylic group of one amino acid and a hydrogen atom is lost from an amine group of another amino acid
  • the carbon double bonded with oxygen from the first amino acid bonds to the nitrogen of the second amino acid
  • this is a condensation reaction so water is released, the resulting molecule is a dipeptide
  • during hydrolysis reactions polypeptides are broken down to amino acids when the addition of water rbeaks the peptide bonds
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

describe the secondary structure and the two shapes that can form within the proteins

A
  • the secondary structure occurs when the weak negatively charged nitrogen and oxygen atoms interact with the weak positively charged hydrogen atoms to form hydrogen bonds
  • alpha-helix and beta-pleated sheet are the two shapes that can form within proteins due to the hydrogen bonds

BETA PLEATED SHEET
- forms when the protein folds so that two parts of the polypeptide chain are parallel to each other enabling hydrogen bonds to form between parallel peptide bonds

ALPHA-HELIX
- occurs when the hydrogen bonds form between every fourth peptide bond (between the oxygen of the carboxyl group and hydrogen of the amine group)

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

describe the three stages in cell fractionation

A

HOMOGENISATION

  • breaking up of cells
  • sample of tissue is placed in a cold isotonic buffer solution
  • ice cold = reduce activity of enzymes that break down organellses
  • isotonic = same water potential as tissue to prevent osmosis and water damage
  • buffered = to prevent organelle proteins from becoming denatures
  • tissue containing solution is then homogenised using a homogeniser
  • homogenisers are a blender like machine that grinds up cells which breaks the plasma membrane of the cells and releases the organelles into a solution called the homogenate

FILTRATION

  • the homogenate is then filtered through a gauze
  • this separates any large cell debris or tissue debris that were not broken up leaving a solution that contains a mixture of organelles

ULTRACENTRIFUGATION
- the filtrate is placed in a tube which is then placed in a centrifuge (machine that separates materials by spinning)

  • the filtrate is first spun at a low speed causing the largest, heaviest organelles to settle at the bottom of the tube where they form a thick sediment known as a pellet
  • the rest of the organelles stay suspended in the solution above, this is known as the supernatant
  • the supernatant is drained off and placed into another tube which is spun at a higher speed causing the heavier organells like mitochondria to settle at the bottom of the tube forming a new pellet
  • the new supernatant is drained off and placed inot another tube which is spun at an even higher speed
  • this process is repeated at increasing speeds until all the different types of organelle present are separated out
  • each new pellet formed contains a lighter organelle than the previous pellet
  • order of mass from heaviest to lightest is
    nuclei, chloroplasts, mitochondria, lysosomes, endoplasmic reticulum, ribosomes
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

describe the three stages in cell fractionation

A

HOMOGENISATION

  • breaking up of cells
  • sample of tissue is placed in a cold isotonic buffer solution
  • ice cold = reduce activity of enzymes that break down organellses
  • isotonic = same water potential as tissue to prevent osmosis and water damage
  • buffered = to prevent organelle proteins from becoming denatures
  • tissue containing solution is then homogenised using a homogeniser
  • homogenisers are a blender like machine that grinds up cells which breaks the plasma membrane of the cells and releases the organelles into a solution called the homogenate

FILTRATION

  • the homogenate is then filtered through a gauze
  • this separates any large cell debris or tissue debris that were not broken up leaving a solution that contains a mixture of organelles

ULTRACENTRIFUGATION
- the filtrate is placed in a tube which is then placed in a centrifuge (machine that separates materials by spinning)

  • the filtrate is first spun at a low speed causing the largest, heaviest organelles to settle at the bottom of the tube where they form a thick sediment known as a pellet
  • the rest of the organelles stay suspended in the solution above, this is known as the supernatant
  • the supernatant is drained off and placed into another tube which is spun at a higher speed causing the heavier organells like mitochondria to settle at the bottom of the tube forming a new pellet
  • the new supernatant is drained off and placed inot another tube which is spun at an even higher speed
  • this process is repeated at increasing speeds until all the different types of organelle present are separated out
  • each new pellet formed contains a lighter organelle than the previous pellet
  • order of mass from heaviest to lightest is
    nuclei, chloroplasts, mitochondria, lysosomes, endoplasmic reticulum, ribosomes
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

name and describe the purpose of each of the enzymes induced in DNA replication

A

DNA helicase - unzips double helix by breaking the hydrogen bonds which join the two polynucleotide strands together

DNA polymerase -
moves down the molecule and catalyses the formation of a phosphodiester bond between the activated nucleotides (condensation reaction)

DNA ligase - binds the new DNA together

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

What are enzymes and how do reactions happen

A
  • enzymes are biological catalysts. All enzymes are globular proteins with a specific tertiary shape
  • the part of the enzyme that acts as a catalyst is called the active site and the rest of the enzyme is much large and is involved in maintaining the specific shape of the enzyme
  • when a reaction involving an enzyme occurs, a substrate is turned into a product. The substrate can be one or more molecules. The active site of an Enzyme is complementary to the substrate it catalyses
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

name all the biological molecules food tests and describe how to carry them out as well as what the results look like

A

BENEDICTS TEST FOR REDUCING SUGARS

  • add benedicts reagent (blue) to the sample in a test tube making sure there is an excess
  • heat the mixture in a water bath for a few minutes
  • a positive test will lie along the scale from blue (no reducing sugar) through green, yellow, orange and a brown/brick red (high concentration of reducing sugar)

TEST FOR NON-REDUCING SUGARS
-add dilute hydrochloric acid to the sample and heat in a water bath that has be brought to a boil
- neutralise the solution with sodium hydrogencarbonate and add a bit more until the solution becomes slightly alkaline (monitor this using a suitable indicator)
- then carry out the benedicts test as normal
= if a colour change occurs then a non reducing sugar is present

IODINE TEST FOR STARCH

  • add a few drops of orange/brown iodine in potassium iodide
  • if starch is present the solution will turn a blue-black colour

EMULSION TEST FOR LIPIDS

  • add ethanol to the sample being tested, shake to mix then add the mixture to a test tube of water
  • if lipids are present a milky emulsion will form
  • if no lipid is present the solution remains clear

BIURET TEST FOR PROTEINS

  • a liquid solution of a sample is treated with sodium or potassium hydroxide to make the solution alkaline
  • then add a few drops of copper (II) sulfate solution (blue) to the solution
  • if a colour change is observed from blue to lilac/purple then proteins are present
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

describe the structure of a DNA nucleotide

A
  • nucleotides contain a deoxyribose sugar with hydrogen at the 2’ position
  • a phosphate group
  • one of the four nitrogenous bases
    adenine and guanine (purine-double ring structure)
    and cytosine and thymine (pyrimidines-single ring structure)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

describe the basic structure for DNA nucleotides

A

DNA nucleotides contain :

  • deoxyribose sugar with hydrogen at the 2’ position
  • a phosphate group
  • one of the four nitrogenous bases: adenine, guanine (purine-two ring structure) and thymine and cytosine (pyrimidines - single ring structure)
16
Q

describe the structure of DNA

A
  • made up of two polynucleotide strands which are antiparallel (run in opposite directions)
    one strand is known as the 5’ to 3’ strand and the other is known as the 3’ to 5’ strand
  • each polynucleotide strand is made up of alternating deoxyribose sugars and phosphate groups bonded together to form the sugar phosphate backbone (these bonds are covalent and phosphodiester)
  • the phosphodiester bonds ling the 5-carbon of one deoxyribose sugar molecule to the phosphate group from the same nucleotide which is then linked by another phosphodiester bond to the 3-carbon of the deoxyribose sugar molecule of the next nucleotide
  • the nitrogenous bases of each nucleotide project out from the backbone towards the interior of the double-stranded DNA
17
Q

What are the similarities and differences between ATP and a DNA nucleotide

A

SIMILARITIES

  • both have a 5 carbon sugar (pentose sugar)
  • both contain a phosphate
  • both contain adenine

DIFFERENCES

  • DNA has a deoxyribose sugar whereas ATP has a ribose sugar
  • DNA can involve all four bases, ATP only adenine
  • DNA has 1 phosphate, ATP has three phosphates
18
Q

state the functions of organelles in eukaryotic cells

A

cell surface membrane - controls the exchange of materials between the internal cell environment and the external environment

cell wall - offers structural support to cell

nucleus - contains genetic material of the cell

nuclear pores - allowing mRNA and ribosomes to travel out of the nucleus and allows enzymes and signalling molecules to travel in

mitochondria - site of aerobic respiration within eukaryotic cells, produces ATP in the cristae

chloroplasts - site of photosynthesis, gives plants its green colour

ribosomes - site of proteins synthesis

endoplasmic reticulum - smooth (involved in the production, processing and storage of lipids, carbohydrates and steroids) and rough (covered in ribosomes and processes proteins made by the ribosomes)

golgi apparatus - modifies proteins and lipids before packaging them into golgi vesicles

large permanent vacuole -

vesicle - membrane bound sac for transport and storage

lysosome - breaks down waste materials such as worn-out organelles using hydrolytic enzymes

centriole - organises the spindle fibres during cell division

microtubules - makes up the cytoskeleton of the cell and is used to provide support and movement of the cell

microvilli - cell membrane projections that increase the surface area for absorption

cilia - hair like projections which allows the movement of substances over the cell surface

flagella - contract to provide cell movement (e.g. sperm)

19
Q

what are the differences between prokaryotic and eukaryotic cells

A

SIZE

  • prokaryotes = 0.5 - 5um in diameter
  • eukaryotes = up to 40um diameter

GENOME

  • prokaryotes = DNA circular with no proteins in cytoplasm
  • eukaryotes = DNA associated with histones (proteins) formed into chromosomes

CELL DIVISION

  • prokaryotes = occurs by binary fission and no spindle involved
  • eukaryotes = occurs by mitosis or meiosis and involves a spindle to separate chromosomes

RIBOSOMES

  • prokaryotes = 70s ribosomes
  • eukaryotes = 80s ribosomes

ORGANELLES
-prokaryotes = very few/no membrane bound organelles
-eukaryotic cells = lysosomes, golgi complex, vacuoles (single membranes)
nucleus, mitochondria, chloroplasts (double membranes)
ribosomes, centrioles, microtubules (no membrane)

CELL WALL

  • prokaryotes = made of peptidoglycan (polysaccharide and amino acids) and murein
  • eukaryotes = present in plants (made of cellulose or lignin) and fungi (made of chitin - cellulose containing nitrogen)
20
Q

what are the factors affecting the rate of reactions

A

TEMP-

  • lower temp = prevents reactions or slows them down
  • higher temp = speeds up reactions
  • higher temp increase = denatures enzymes breaking bonds causing the tertiary structure of the protein to change which permanently damages active site

pH -

  • extreme pH conditions cause enzymes to denature
  • this is because solutions with an excess of H+ ions (acidic) and OH- ions (alkaline) can cause the bonds that hold the tertiary structure of a protein to break

ENZYME INHIBITORS -

  • competitive inhibitors have a similar shape to that of the substrate molecules and therefore compete with the substrate for the active site
  • non-competitive inhibitors bind to the enzyme at an alternative site which alters the shape of the active site and therefore prevents the substrate from binding to it
21
Q

why are sodium ions important

A

sodium is an inorganic ion and is required for the transport of lucose and amino acids across cell-surface membranes

  • glucose and amino acid molecules can only enter cells through carrier proteins alongside Na+ this is called co-transport

CO TRANSPORT

  • first, Na+ is actively transported out of the epithilial cells that line the villi
  • The Na+ concentration inside the epithilial cells is now lower than the Na+ concentration in the lumen of the small intestine
  • Na+ now re-enters the cells through co-transport proteins on the surface membrane of the epithilial cells, allowing glucose and amino acids to enter at the same time
  • Na+ is also required for the transmission of nerve impuleses