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Biological Molecules Flashcards

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1
Q

Key biological molecules

A

Fe N C H O P S

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2
Q

What elements make up Lipids

A

Carbon hydrogen and oxygen

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3
Q

What elements make up nucleic acids

A

C H N O P

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4
Q

What defines a polar molecule

A

A molecule with areas of electron negativity and positivity

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5
Q

Properties of water

A

High latent heat of vapourisation
High surface tensions
Polar molecule
Denser as it gets colder

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6
Q

Properties of water

A

High latent heat of vapourisation
High surface tensions
Polar molecule
Denser as it gets colder

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7
Q

General formula of glucose

A

CnH2nOn

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8
Q

What type of carbohydrate is glucose

A

A hexose monosaccharide

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9
Q

What is the shape of alpha glucose

A

Down, up, down, down

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10
Q

What is a condensation reaction

A

A reaction where 2 molecules react to form a new molecule and a molecule of water

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11
Q

Name of the Bond formed between 2 alpha glucose molecules

A

1-4 glycocidic bond

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12
Q

Example of a monosaccharide and its formed disaccharide

A

Fructose -> sucrose

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13
Q

How is starch produced

A

The bonding of the polysaccharide amylose (formed from alpha glucose molecules) which is further stabilised by intermolecular hydrogen bonding to make it more compact and less soluble

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14
Q

What is the other possible form of starch

A

Amylopectin ( formed by 1-6 glycocidic bonds )

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15
Q

How does cellulose form

A

Alternate beta glucose molecules are turned upside down
Cellulose molecules are then joined by hydrogen bonds to make micro fibrils which join to make macrofibrils which are strong and insoluble and used to make cell walls

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16
Q

Chemical test for reducing sugars

A

Add Benedict’s reagent and heat in a water bath at 70 degrees
A precipitate will form on the scale of blue, green, yellow, brown and brick red, which indicated Cu+ ion concentration

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17
Q

Test for non reducing sugars

A

Add HCl first to hydrolyse the solution into glucose and fructose

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18
Q

What are biosensors

A

Use biological components to determine the presence and concentration of glucose.
Involves:
Molecular recognition - a protein or antibody is immobilised to a surface
Transduction - a change occurs in a transducer which detects a change e.g. in pH levels and produce a response concordant with that change such as the release of an immobilised dye or an electric current
Display - This produces a visible quant/qualitative response

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19
Q

What are Lipids

A

Molecules made of carbon oxygen and hydrogen
Non polar due to an even distribution of electrons
Large and complex ( macromolecules ) made from monomers

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20
Q

Triglycerides

A

One glycerol combined with 3 fatty acids
(One alcohol combined with 3 carboxylic acids)
OH groups interact leading to the formation of 3 H2O molecules + bonds between the fatty acids and the glycerol ( ester bonds ) - esterification -

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21
Q

Saturated meaning

A

No double bonds within a molecule

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22
Q

Unsaturated meaning

A

Presence of double bonds within a molecule

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23
Q

Unsaturated fat characteristics

A

Liquid at room temperature ( oils etc )

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24
Q

Saturated fat properties

A

Solid at room temperature

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25
What are phospholipids
Modified triglycerides contains a phosphate group and 2 fatty acids Phosphate ions are found in the cytoplasm of every cell and are soluble in water due to their extra electron which gives them a negative charge Have non polar tails (hydrophobic) and polar heads (hydrophilic)
26
What do phospholipids form on contact with water
A phospholipids bi layer
27
What are sterols
Steroid alcahols that are neither fats or oils but instead complex alcohol molecules based on a 4 carbon ring structure with an OH group With hydrophobic and Phyllic (due to the OH) characteristics
28
What is cholesterol
A sterol produced in the liver and intestines that helps form cell membranes and maintain their structural integrity
29
What are the roles of lipids
Membrane/hydrophobic barrier formation Hormone production Electrical insulation Waterproofing Thermal insulation Cushioning of vital organs Buoyancy for aquatic animals
30
How has health advice changed in respect to lipids
Saturated fats do not cause heart disease
31
What are the structures of proteins
Poly peptides containing chains of amino acids
32
Amino acid structure
Amine group, R-group, Carboxyl group
33
How do amino acids form proteins
By folding and an interaction with R-groups
34
Levels of protein structure
Primary-Single polypeptide chain Secondary-folding into alpha helix or beta pleated sheets Tertiary-R groups begin to interact = hydrophilic/phobic interactions, hydrogen bonds, ionic bonds, disulfide bridges Quaternary- interactions between proteins
35
36
How to test for proteins
Biurets test Add NaOH Add CU(II)SO4 Will go from blue to violet
37
What are the types of proteins
Globular Conjugated Fibrous
38
What are Globular proteins
Proteins that are compact, water soluble and roughly spherical with hydrophilic r groups on the outside of the protein so they are soluble Important for chemical reactions, immunity and muscle contraction
39
Conjugated proteins
Globular proteins with a non protein component ( a prosthetic group ) such as a metal ion or a molecule derived from a vitamin
40
Fibrous proteins
Formed from long insoluble molecules with hydrophobic r groups on their outside surface, making them insoluble
41
Elastin
Linking many soluble tropoelastin molecules Stabilised by cross link covalent bonds Still has flexibility
42
Collagen
3 polypeptide chains Glycine is every third amino acid =Closely packed triple helix Many hydrogen bonds=long quaternary proteins With tropocollagen cross links=strengtyh
43
What are nucleic acids made up of
Carbon, Hydrogen, Oxygen, Nitrogen and Phosphorous
44
Components of a nucleotide
Pentose sugar Phosphate group Nitrogenous base
45
How are nucleotides joined together
Condensation reactions forming phosphodiester bonds
46
Pyramidine bases
( single ring ) Thymine and Cytosine
47
Purine
( double ring ) Adenine and Guanine
48
How do bases pair
In a complimentary fashion A-T C-G With hydrogen bonds forming between them
49
What is semi conservative DNA replication
2 new molecules of DNA get produced with each one containing a strand of the origional DNA
50
Roles of enzymes in DNA replication
DNA helicase breaks down the hydrogen bonds between the strands of DNA DNA polymerase catalyses the formation of the phosphodiester bonds between nucleotides
51
What is a triplet of nucleotides known as
A codon
52
Transcription
DNA unwinds and unzips with DNA helicase Antisense strand acts as the template strand so the complimentary RNA has the same sequence as the sense strand Free RNA nucleotides bind to the antisense strand (complimentary order) Phosphodiester bonds formed between the RNA nucleotides by RNA polymerase mRNA is formed
53
Why are transcription and translation important
As otherwise DNA would be unreplecatable as it is too long to be able to leave via the nucleur pores
54
Translation
mRNA binds to a specific site on a ribosome before it is decoded into an amino acid sequence tRNA contains anticodons which bind to complimentary codons on the mRNA and bring specific amino acids in the correct order
55
What is ATP
Adenosine Tri phosphate
56
What is the role of ATP
As an energy source for muscle contraction, cell division and nerve impulse transmission
57
Why do cells require energy
Synthesis Transport (of molecules) Movement
58
How does ATP release energy
By the breaking of the bond to the last phosphate group via hydrolysis to make adenosine di phosphate and a phosphate group
59
Lock and key hypothesis
Substrate is exactly specific to the active site of the enzyme to make an enzyme-substrate complex
60
Induced fit hypothesis
Enzymes active sight slightly changes shape to mould to the substrate and place further strain on its bonds
61
Intracelullar enzymes
Essential role in the function of cells such as the synthesis/breakdown of molecules E.g. H2O2
62
Extracellular enzymes
Suppliers of raw materials to cells to sustain the demand
63
What are thermophiles
Organisms designed to live in extreme temperatures
64
What is a serial dilution
Stepwise dilution of a stock of known concentration
65
Competitive inhibitor
An enzyme inhibitor that acts on the active site of the enzyme, changing its shape and preventing a substrate from binding
66
Non-competitive inhibitor
Inhibitor that binds to another part of the enzyme and permenantly denatures the shape of the active site
67
What’s a cofactor
A non-protein helper that helps transfer atoms or groups Obtained from diet as minerals such as Cl- ions and amylase
68
What’s a coenzyme
An organic cofactor Derived from vitamins E.g. vit B3 -> NAD -> H atom transferal
69
What’s a prosthetic group
Cofactors that are required by certain enzymes to allow for them to perform their function Like Zn2+ ions to help with carbonic a hydrate to metabolis CO2 Or Fe in haemoglobin
70
What is precursor activation
Precursor enzymes need to undergo a change in shape to be able to perform their function So a cofactor must be added to make a holo enzyme
71

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