Snab Biology - Topic 2: 'genes And Health'

Front 1

Amino acid structure:

Back 1

An alpha carbon surrounded by a carboxylic acid group, an amine group, a hydrogen, and an R group.

Front 2

Primary structure is:

Back 2

The sequence of amino acids in the polypeptide chain.

Front 3

Amino acids are joined by:

Back 3

Peptide bonds.

Front 4

Secondary structure is:

Back 4

The formation of alpha-helices and beta-pleated sheets due to hydrogen bonding.

Front 5

Tertiary structure is:

Back 5

The three-dimensional shape of a polypeptide chain due to hydrophobic and hydrophilic interaction and interaction of the chain with itself.

Front 6

Directions causing tertiary structure include:

Back 6

Hydrogen bonds, Ionic bonds, covalent bonds, and polar interactions. Hydrophobic and hydrophilic interactions also shape the molecule.

Front 7

Quaternary structure is:

Back 7

The shape of two or more polypeptide chains held together by hydrogen bonds.

Front 8

Proteins can be broken down by:

Back 8

Hydrolysing the peptide bonds.

Front 9

Proteins can be denatured by:

Back 9

Unusual pH or temperatures.

Front 10

Catalysts are:

Back 10

Chemicals which can accelerate a given reaction, often with a route of lower activation enthalpy, and emerge unchanged at the end.

Front 11

An enzyme is:

Back 11

A type of globular protein acting as a biological catalyst. It has an active site for a specific substrate.

Front 12

The lock and key hypothesis is:

Back 12

The idea of close interaction between complementary enzymes and substrates.

Front 13

The induced fit theory is:

Back 13

The idea that a substrate causes the enzyme to assume the right shape.

Front 14

The lock and key hypothesis sequence:

Back 14

Front 15

The lock and key hypothesis sequence:

Back 15

Front 16

To start a reaction, bonds must be broken by:

Back 16

Adding heat energy or a catalyst for that reaction.

Front 17

Enzyme concentration and rate of reaction:

Back 17

The rate increases as more enzyme is added, up to the point where all substrate is being catalysed immediately, and the graph levels off.

Front 18

Phospholipid structure:

Back 18

A phosphate (hydrophilic) head attached to a glycerol and two (hydrophobic) fatty acid chains.

Front 19

Evidence for the fluid mosaic:

Back 19

Phospholipids are polar. They also naturally form micelles and layers in water. Comparison of monolayer and surface areas of cells. Proteins can be seen with an electron microscope.

Front 20

Phospholipid structure:

Back 20

A phosphate (hydrophilic) head attached to a glycerol and two (hydrophobic) fatty acid chains.

Front 21

Evidence for the fluid mosaic:

Back 21

Phospholipids are polar. They also naturally form micelles and layers in water. Comparison of monolayer and surface areas of cells. Proteins can be seen with an electron microscope.

Front 22

What can pass through a cell membrane easily?

Back 22

Lipid-soluble substances can easily pass through the membrane. Polar and charged molecules require transport.

Front 23

Evidence for the fluid mosaic:

Back 23

Phospholipids are polar. They also naturally form micelles and layers in water. Comparison of monolayer and surface areas of cells. Proteins can be seen with an electron microscope.

Front 24

What can pass through a cell membrane easily?

Back 24

Lipid-soluble substances can easily pass through the membrane. Polar and charged molecules require transport.

Front 25

The fluid mosaic:

Back 25

Front 26

Evidence for the fluid mosaic:

Back 26

Phospholipids are polar. They also naturally form micelles and layers in water. Comparison of monolayer and surface areas of cells. Proteins can be seen with an electron microscope.

Front 27

The fluid mosaic:

Front 28

Glycoproteins are:

Back 28

Forked

Front 29

Evidence for the fluid mosaic:

Back 29

Phospholipids are polar. They also naturally form micelles and layers in water. Comparison of monolayer and surface areas of cells. Proteins can be seen with an electron microscope.

Front 30

The fluid mosaic:

Back 30

Front 31

What can pass through a cell membrane easily?

Back 31

Lipid-soluble substances can easily pass through the membrane. Polar and charged molecules require transport.

Front 32

Glycoproteins are:

Back 32

Forked

Front 33

Glycolipids are:

Back 33

Straight.

Front 34

Evidence for the fluid mosaic:

Back 34

Phospholipids are polar. They also naturally form micelles and layers in water. Comparison of monolayer and surface areas of cells. Proteins can be seen with an electron microscope.

Front 35

What can pass through a cell membrane easily?

Back 35

Lipid-soluble substances can easily pass through the membrane. Polar and charged molecules require transport.

Front 36

The fluid mosaic:

Back 36

Front 37

Glycoproteins are:

Back 37

Forked

Front 38

Glycolipids are:

Back 38

Straight.

Front 39

Structures in a cell membrane:

Back 39

The bilayer, proteins (channel, transmembrane, etc.), cholesterol, glycolipids, glycoproteins.

Front 40

The membrane can be found:

Back 40

Around cells and within them (organelles)

Front 41

Diffusion:

Back 41

The movement of small and/or lipid-soluble molecules directly through the cell membrane. Passive and therefore down the concentration gradient.

Front 42

Facilitated diffusion:

Back 42

The movement of any (inc. polar and charged) molecules through channel proteins. Passive.

Front 43

Osmosis:

Back 43

The diffusion of free water molecules through a partially permeable membrane. From areas of low to high solute concentration or inv. water conc.

Front 44

Active transport:

Back 44

The movement of any molecule via carrier protein using ATP. can be done against a concentration gradient actively.

Front 45

Exo/endo-cytosis:

Back 45

The transport of any large particle using vesicles in or out of the cell.

Front 46

Beetroot practical procedure:

Back 46

Cut equal sizes of tissue. Rinse to remove excess pigment. Immerse in equal volumes of /thing tested/ for equal amount of time. Gently remove slices and agitate solution. Place solution in colorimeter and plot light transmittance against other variable.

Front 47

Nucleotides are comprised of:

Back 47

A phosphate group, a deoxyribose sugar, and a base.

Front 48

Nucleotides are joined by:

Back 48

Condensation reactions forming phosphodiester bonds.

Front 49

Bases are joined by:

Back 49

Complementary base pairing through hydrogen bonds.

Front 50

Adenine pairs with:

Back 50

Thymine.

Front 51

Cytosine pairs with:

Back 51

Guanine.

Front 52

Uracil replaces x in mRNA.

Back 52

Thymine. A pairs with U to make gold.

Front 53

A and G are:

Back 53

Larger purine bases.

Front 54

C and T are:

Back 54

Smaller pyramidine bases.

Front 55

The genetic code is:

Back 55

The order of bases on one strand of DNA.

Front 56

Amino acids are coded for by:

Back 56

The sequence of triplets in a gene.

Front 57

A gene is:

Back 57

The sequence of bases on one DNA strand coding for a single polypeptide chain.

Front 58

mRNA is used:

Back 58

In transcription to compliment the genetic code, and transport the code to a ribosome. It is there used in translation with tRNA to create polypeptides.

Front 59

Meselson and Stahl proved that:

Back 59

DNA replication is semi-conservative.

Front 60

DNA replication sequence:

Back 60

The DNA strands unwind and split. Free nucleotide bases then attach to complementary bases on the two strands through hydrogen bonding. DNA polymerase joins the free bases with phosphodiester bonds. Two (hopefully) identical new strands result.

Front 61

mRNA is used:

Back 61

In transcription to compliment the genetic code, and transport the code to a ribosome. It is there used in translation with tRNA to create polypeptides.

Front 62

Meselson and Stahl proved that:

Back 62

DNA replication is semi-conservative.

Front 63

DNA replication sequence:

Back 63

The DNA strands unwind and split. Free nucleotide bases then attach to complementary bases on the two strands through hydrogen bonding. DNA polymerase joins the free bases with phosphodiester bonds. Two (hopefully) identical new strands result.

Front 64

The two stages of protein synthesis are:

Back 64

Transcription and translation.

Front 65

Transcription:

Back 65

Occurs in the nucleus where mRNA is made to copy DNA. The mRNA then exits the nucleus through nuclear pores. The DNA template (antisense) strand is used to create mRNA through complementary bases. The mRNA bases are joined by RNA polymerase.

Front 66

Translation:

Back 66

After exiting the nucleus into the cytoplasm, the mRNA reaches a ribosome where tRNA brings amino acids to a complementary triplet (codons) on the mRNA with the tRNA anticodons.

Front 67

Codons belong to:

Back 67

mRNA triplets.

Front 68

Anticodons belong to:

Back 68

tRNA triplets.