Chapter 3- Biological Molecules and Chapter 4- Enzymes Flashcards

1
Q

How does hydrogen bonding occur in water?

A

H2O is a polar molecule

different molecules of water interact between positive and negative ends

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2
Q

What are carbohydrates made up of?

A

C,H,O

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3
Q

What are lipids made up of?

A

C,H,O

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4
Q

What are proteins made up of?

A

C,H,O,N,S

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5
Q

What are nucleic acids made up of?

A

C,H,O,N,P

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6
Q

Structure of glucose

A

Glucose is a monosaccharide, composed of six carbons and therefore a hexose monosaccharide, when forming a polymer creates a polysaccharide

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7
Q

What is an alpha glucose

A

Hydroxyl group on same side

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8
Q

What is a beta glucose?

A

Hydroxyl group above not below on 1st carbon

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9
Q

Properties of glucose

A

Polar and soluble in water

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10
Q

What do two glucose molecules form

A

Forms maltose and water

Maltose contains a 1,4 glycosidic bond

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11
Q

Other hexose monosaccharides

A

Fructose and galactose

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12
Q

What forms sucrose?

A

Fructose + glucose

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13
Q

What forms lactose?

A

Galactose + glucose

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14
Q

Two important pentose sugars

A

Ribose sugar

Deoxyribose sugar

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15
Q

Difference between a hexose and pentose monosaccharide

A

Hexose contains 6 carbons

Pentose contains 5 carbons

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16
Q

How is starch formed?

A

Formed by many alpha glucose molecules
One of the polysaccharides in starch is called amylose. Amylose is formed by alpha glucose molecules joined together only be 1,4 glycosidic bonds. The angle of the bond means that this long chain of glucose twists to form a helix which is further stabilises by hydrogen bonding. This makes the polysaccharide more compact , and much less soluble

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17
Q

What other type of starch can be formed?

A

When 1,6 glycosidic binds form , this starch is known as amylopectin

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18
Q

Key properties of amylopectin and glycogen

A

Insoluble, Branched, and compact

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19
Q

Hydrolysis reaction

A

Addition of water molecules

Converts starch to glucose

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20
Q

Cellulose structure and how it’s formed

A

Beta glucose molecules , alternate beta glucose molecule turned upside down.
Unable to coil or branch
Cellulose make hydrogen bonds with each other forming microfibrils, there microfibrils combine to produce fibres. These fibres are strong and are used to make cell walls.

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21
Q

Roles of glycogen and amylopectin

A

Insoluble, Branched and compact. These properties mean it is ideally suited to the storage roles that they carry out

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22
Q

What is a triglyceride made up of?

A

One glycerol molecule

Three fatty acids

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23
Q

What is a phospholipid made up of?

A

Phosphate group
Two fatty acids
Glycerol molecule
The phosphate ions have extra electrons so are negatively charged making them soluble in water.

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24
Q

Roles of lipids

A

Membrane formation
Hormone production
Electrical insulation
Waterproofing

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25
Synthesis of peptides
Amino acids join when the amine and carboxylic acid groups connected to the central carbon atoms react. The r groups are not involved at this point. The hydroxyl in the carboxylic acid group of one amino acid reacts with a hydrogen in the amine group of another amino acid. A peptide bond is formed between two amino acids
26
Primary structure
Sequence in which the amino acids are joined. It is directed by information carried within DNA. The particular amino acids in the sequence will influence how the polypeptide folds to give the proteins final shape.The only bonds involved in primary structure are peptide bonds.
27
Secondary structure
The oxygen, hydrogen and nitrogen atoms of the basic , repeating structure of amino acids interact. Hydrogen bonds may form within the amino acid chai, pulling it in to a coiled shape called an alpha helix. Can also form beta pleated sheets.
28
Tertiary structure
``` Folding of the protein into its final shape Interaction between r groups Hydrophobic and hydrophilic interactions Hydrogen bonds Ionic bonds Disulfide bonds ```
29
Quaternary structure
The association of two or more individual proteins called subunits
30
Breakdown of peptides
Requires addition of a water molecule
31
Globular protiens
Compact water soluble and usually roughly spherical in shape. They form when proteins fold into their tertiary structure in such a way that the hydrophobic r groups on the amino acids are kept away from the aqueous environment
32
Haemoglobin
Red oxygen carrying pigment found in red blood cells Made up of four polypeptides Two alpha and two beta subunits Each subunit contains a prosthetic haem group Able to pick up oxygen
33
Catalase
An enzyme which speeds up the breakdown of hydrogen peroxide
34
Fibrous protiens
Formed from long insoluble molecules. This is due to the presence of a high proportion of amino acids with hydrophobic r groups in their primary structures. They contain a limited range of amino acids, usually with small r groups. Primary structure usually quite repetitive. They tend to make strong, long molecules which are not folded into 3D shapes.
35
Keratin
A group of fibrous protiens present in hair, skin and nails. Contains many strong disulphides bridges
36
Elastin
Fibrous protein found in elastic fibres. Elastic fibres are present in the walls of blood vessels and in the alveoli of the lungs.
37
Collagen
Is another fibrous protien. It is a connective tissue found in skin, tendons, ligaments and the nervous system Has a strong rope like structure and is long.
38
What does a nucleotide contain?
A pentose monosaccharide A phosphate group A nitrogenous base
39
How are nucleotides linked together?
By phosphodiester bonds
40
Difference between deoxyribose and ribose
Deoxyribose contains one less oxygen
41
Description of DNA
Made up of two strands of polynucleotides coiled into a helix The two strands of double helix joined together by hydrogen bonds Run in opposite directions-anti parrallel
42
Different number of bonds between C and G , A and T
C and G 3 bonds | A and T 2 bonds
43
What bases are pyrimidines
Cytosine and Guanine
44
What bases are purines?
Anadine and guanine
45
How does RNA differ from DNA
Ribose, U instead of A
46
What does semi conservative replication mean
One old strand, one new | Double helix is unzipped, the free dna nucleotides will pair with complimentary base pairs.
47
Role of DNA helicase
Breaks down the hydrogen bonds
48
Role of DNA polymerase
Forms phosphodiester bonds
49
What enzyme breaks down start to maltose
Amylase
50
What enzyme breaks down maltose to glucose?
Maltose
51
What enzyme breaks down hydrogen peroxide?
Catalase
52
Enzyme to breakdown proteins into smaller peptides
Trypsin
53
What is temperature coefficient?
Measure of how much the rate of reaction increases with a 10 degrees rise in temperature.
54
How are enzymes affected by temperature?
As the temperature increases the vibrations increase until the bonds strain and then break. The breaking of these bonds results in a change in the precise tertiary structure of the protien. The enzyme has changed shape and is said to have been denatured.
55
How does pH affect enzyme activity?
Hydrogen bonds ams ionic bonds between amino acid r groups hold protiens in their precise 3D shape. A change in pH refers to a change in hydrogen ion concentration. More hydrogen ions are present in low pH acid environments and fewer hydrogen ions are present in high pH alkaline environments
56
What is competitive inhibition?
A molecule that has similar shape to substrate of enzyme and can fit into active site Blocks the substrate from entering the active site The enzyme cannot carry out its function and is said to be inhibited
57
What is non competitive inhibition?
Inhibitor binds to the enzyme at a location other than the active site. Known as a allosteric site.
58
Define a cofactors
A non protien helper component in order to carry out their function as biological catalysts. They may transfer atoms or groups from one reaction to another in a multi step pathway or they may actually for, part of the active site of an enzyme
59
What is a prosthetic group?
Required by certain enzymes to carry out the catalytic function
60
In what reaction are zinc ions important?
Form an important part of the structure of carbonic anhydrase an enzyme necessary for metabolism of CO2
61
How does hydrogen bonding occur in water
The O takes a negative charge The two Hydrogens take a positive charge The hydrogens are attracted to other oxygens from other water molecules
62
Roles of water
Solvent Transport medium Coolant A habitat
63
Benedictus test for reducing sugars
``` Place sample in boiling tube Add an equal volume of benedict reagent Heat the mixture gently for 5 minutes A brick red precipitate forms if positive and reduces Cu2+ to Cu+ A blue precipitate forms if negative ```
64
Benedictus test for non reducing sugars
Sucrose is an example | However if sucrose is heated with HCl first it is hydrolysed glucose and fructose which are both reducing sugars
65
Iodine test
A few drops of iodine dissolved in potassium iodide solution are mixed with a sample. If the solution changes from yellow/brown to purple/black starch is present
66
What is a colorimeter?
A piece of equipment used to quantitvely measure the absorbance, or transmission, of light by a coloured solution. The more concentrated the solution the more light it will absorb and less it will transmit.
67
What is a biosensor?
Use biological components to determine the presence and concentration of molecules such as glucose Molecular recognition Transduction
68
Thin layer chromatography method
Draw a pencil line on the chromatography plate about 2cm above from the bottom. Four equally spaced points are marked along the pencil line The amino acid solution is added to a spot on the pencil line using a capillary tube The three remaining marks were spotted with three known amino acids Plate was then placed into a jar containing the solvent. The plate was then left until the solvent was 2cm from the top The plate was then allowed to dry The plate is then sprayed with ninhydrn spray
69
Define genetic code
DNA must code for a sequence of amino acids
70
Define a triplet code
A sequence of three bases, called a codon. Each codon codes for a amino acid A section of DNA which codes for a whole protien is known as a gene It is universal all organisms use this code
71
Define Degenerate code
Stop codons Start codons Several codons code for same amino acid
72
Precursor activation
When enzyme is produced in an inactive form. Precursor enzymes often have to undergo a change in shape to the tertiary structure, particularly to the active site , to be activated. This can be achieved by the addition of a co factor.
73
Examples of fibrous proteins
Keratin Elastin Collagen
74
Structure of elastin
Link many soluble tropoastin Makes a cross linked stable insoluble structure Able to stretch and recoil without breaking
75
Structure of collagen
Three polypeptide chains wound around each other forms a triple helix structure Every third amino acid in chain is glycine Many boyfriends bonds form between the polypeptide chains forming long quaternary proteins Produce strong fibers The r groups repel one another increasing stability
76
Lipid emulsion test
``` Sample mixed with ethanol Then water Shaken If white emulsion forms indicates present of lipid If remains clear negative ```
77
Identifications of proteins
Bitter test 3cm of liquid sample mixed with an equal volume of sodium hydroxide 1% copper sulfate solution was then added a few drops at a time until the sample turned blue The solution was mixed and left to stand for five minuteman minutes