Biochemistry Flashcards
1
Q
Functions of carbohydrates
A
1) they store energy
2) the are structural
2
Q
The chemical structure of carbohydrates
A
Carbon:hydrogen:oxygen
1. 2. 1
3
Q
Types of cerbohydrates
A
Monosaccharides: simple ring sugars, glucose and fructose.
Disaccharides: two monosaccharides combined, sucrose and lactose.
Polysaccharides: polymer(long chains of repeating units) of monosaccharides.
4
Q
What kids of energy do polysaccharides store?
A
Starch in plants
Glycogen in animals
5
Q
Polysaccharides
Cellulose
Chitin
A
Polysaccharides are also structural molecules
Cellulose makes up cell wall plants
Chitin makes up exoskeleton, cell walls of fungi
6
Q
Glucose
A
It is dissolved in water and it is almost always in ring form, but dry. Glucose can have a linear structure.
(Look at photo in notes)
7
Q
What is the difference of alpha glucose and beta glucose?
A
They are isomers and on alpha glucose on the 4th carbon the hydroxyl group is-on the bottom.
beta glucose on the 4th carbon the hydroxyl group is at the top
8
Q
Glycoside bonds
A
There are two types of glycoside bonds, Alpha and Beta bonds.
Starch is bonded by 1-4 glycoside bonds. (Image in notes).
Starch is 1-4 linkage of alpha glucose monomers.
9
Q
Cellulose
A
It is polymer of beta glucose together by beta 1-4 glycoside linkages. (Diagram in notes)
10
Q
The four major classes of biomolecules!
A
All living things are made up of four classes of biological molecules which are
Carbohydrates
Lipids
Protein
Nucleic acid
11
Q
Macromolecules
A
They are large molecules composed of thousands covalently bounded atoms.
Molecular structures and functions are inseperated.
They are e
12
Q
Macromolecules
A
They are large molecules composed of thousands of covalently bonded atoms.
Molecular structures and function are inseperated.
13
Q
Macromolecules continued
A
They are polymers built from monomers
- polymer are small building block molecules consisting of many smaller building blocks they are called monomers.
- three of the four classes of life’s organic molecules are polymers
- carbohydrates
- proteins
- nucleic acid
14
Q
The synthesis and breakdown of polymers.
A
A dehydration reaction occurs when two monomers bond together through the loss of a water molecule.
Polymers are disassembled to monomers by hydrolysis, a reaction that is essentially the reverse of dehydration reaction.
15
Q
Dehydration synthesis
A
Dehydration reaction is synthesizing a polymer.
It also removes a water molecule forming a new bond. ( diagrams in notes)
16
Q
Hydrolysis synthesis
A
This is the breaking down of a polymer.
It also adds a water molecule. ( diagram in notes)
17
Q
The diversity of polymers
A
Each cell has thousands of different macromolecules.
Macromolecules vary among cells of organisms, they vary a lot between species.
*An immense variety of polymers can be built from a small set of monomers
18
Q
Carbohydrates serve as fuel and building material
A
- carbohydrates include sugars and the polymer of sugars
- monosaccharides are the simplest carbohydrates.
- carbohydrate macromolecules are polysaccharides, polymers are composed of many sugar building blocks.
19
Q
Sugars:Monosaccharides
A
- Monosaccharides have molecular formulas that are usually multiplies of CH2O.
- Glucose(C6H12O6) is the most common monosaccharide.
- Monosaccharides are classified by the location of the carbonyl group and the number of carbons in the carbon skeleton.
20
Q
Sugars:Disaccharides
A
- A disaccaride is formed when a dehydration reaction joins two monosaccharides.
- This covalent bond is called a glycosidic linkage.( diagram in notes)
21
Q
Lipids are Hydrophobic
A
> lipids are the one class of large biological molecules that do not form polymer.
> the unfing feature of lipids is having little or no affinity of water.
> because they consist mostly of hydrocarbons which forms no polar covalent bond they are hydrophobic.
> the most important lipids are fats, steroids, and phospholipids.
22
Q
Hydrophobic lipids
A
Hydrophobic lipids are composed of c,H,O and are used for insulation and long term energy storage components of cell membrane.
Fats and oils are made up of subunits- glycerol and fatty acids.
> Waxes: mainly used for covering and protection.
> Steroids: precursors to steroid hormones and fat soluble vitamins.
23
Q
Triglycerides are composed of
A
> Glycerol
- glycerol is a carbon 3 Alcohol - it has three OH groups attached.
> Fatty acids side chain
- a fatty acid chain of carbon atoms with hydrogen atom
- at one end of the chain there is carboxyl group, COOH. (Cheek diagram)
24
Q
Fatty acids composed of
A
> Hydrophobic hydrocarbon chain(tail)
hydrophilic carboxyl acid group(head)
> different fatty acids have different hydrocarbon tails.
25
Triclycerides
An ester link is formed by dehydration synthesis between the glycerol and the fatty acid.
26
Saturated Fats
Contains no double bonds, solid at room temperature.
27
Unsaturated fat
Have double bonds that kink the molecule and they are liquid at room tempurature
28
Phospholipids
Head is hydrophilic and consists of choline,phosphate and glycerol.
>tail is hydrophobic consists of fatty acids.
29
Fats
Fats: are constructed from two types smaller molecules:Glycerol and fatty acids.
>Glycerol is a 3 group carbon alcohol with a hydroxyl group attached to each carbon.
> A fatty acid consists of a carboxyl group attached to a long carbon skeleton. (Check diagram)
30
Dehydration RXN :add a fatty acid
> next add a fatty acid through a dehydration synthesis reaction
> the C double bond O, single bond OH makes it an acid.
31
Dehydration RXN 2
>add a second fatty acid through dehydration synthesis reaction
32
Dehydration reaction three
>the joining of the C of the fatty acid of the O of the hydroxyl group of the glycerol is called and ester linkage. (Check diagram)
33
Fats are insoluble in swipes enviorments
Fats separate from water because Water molecules from hydrogen bonds with each other and exclude fats
34
Saturated or unsaturated
Fats made from saturated fatty acids are called saturated fats and are solid at room temperature.
Most animal fats are saturated
Saturated fatty acids have the maximum number of hydrogen atoms possible and no double bonds.
Check diagram
35
Unsaturated fats
Fats made from unsaturated fatty acids are called unsaturated fats they are liquid at room temperature.
Plant fats and fish fats are usually unsaturated.
They have one or more double bonds.
A rich diet in saturated fat may lead to cardiovascular diseases.
36
Hydrogenation
It is the process of converting unsaturated fats to saturated fats by adding a hydrogen
37
Trans fat
Hydrogenating vegetable oils also creates unsaturated fats with trans double bonds.
These trans fats may contribute more than saturated fats to cardiovascular disease
38
Fats Function
The major function of fats is to store energy
Humans and other mamas store their fat in adipose cells.
Adipose tissue also contains vital organs and insulates the body.
39
Phospholipids
When they are added to water they self assemble into bilayer with hydrophobic tails pointing towards inside.
The structure of phospholipids result in bilayer arrangement found in cell membranes.
40
Steroids
They are lipids characterized by carbon skeleton consisting of four fused rings.
Cholesterol an important steroid is a component in animal cell membrane.
41
Amino acids
All proteins are made up of the same 22 amino acids .
10 amino acids are considered essential (obtained by food)
12 considered non essential(made up by the body)
42
Formation of the peptide bond
Two amino acid molecules : the position of the r groups determines the amino acid.
The molecule must be oriented so that the carbolic acid group of one can react with the amino group.
The petite bond forms with the elimination of water molecule, it is another example of condensation reaction.
43
Protein structure (primary)
Sequence of amino acid (form a polypeptide chain)
44
Secondary structure of protein
Protein chain folds to maximum intermolecular bonding
H bonds are the main force in stabilizing structures
May form alpha helix structure or beta pleated sheets.
45
Tertiary structure of protein
Example is a myoglobin a globular protein
Polarity of amino acid is important in how proteins fold.
46
Quadternary structure of protein
In protein that contain more than one protein chain refers to interaction between.
47
Prosthetic group
Non protein component essential for function
Example hemoglobin
Heme group containing iron is required to bind O2
48
Enzymes
They are molecules that catalyze or speed up the biochemical reactions in living things
Three rules to be an enzyme
Most are proteins
Lower the energy of activation requires for a reaction to occur.
Are not consumed by the reaction
49
Catalyst
They increase the rate of the chemical reaction by lowering the activation energy.
50
Activation energy ( the energy input required to initiate a chemical reaction)
Enzymes interact with substrates
Binding of the enzyme to a substandard cause the enzyme to change shape producing a better induced fit between molecules.
51
Substrates
They are molecules that will undergo a reaction when bound to the enzyme
Enzymes will only interact with specific substrates
The substrate fits into the active site.
The substrate binding causes the enzyme to change shape.
Chainring the shape of an enzyme affects its ability to function.
52
Enzyme naming convention
The first part of an enzyme usually describes the substrate.
The second part of an enzyme usually indicates the type of reaction it will catalyze
Most enzyme names end in suffix - ase
53
How enzymes work
Enzymes makes it easier for chemical reactions to occur
* by destabilizing the bonds in the substrate
* by bringing substrates together so they react
* by decreasing entropy disorder in the system
They make the chemical reactions possible in the cells enviorment
54
How enzymes work continued
Through enzymes cells can carry out anabolic and catabolic reactions and end up with a net profit of energy
Cellular respiration is the process of breaking down glucose and storing the energy excess energy from molecule into a form of energy that is useful for the cell
55
Cells use enzymes to process energy and matter
Reaction that break chemical bonds release their thermal potential energy.
Ex:burning wood
Organisms obtain energy through enzyme catalyze biochemical reactions.
56
Coenzymes and cofactors
Many enzymes require special molecule to help them function correctly.
57
Cofactors
In organic molecules ions, such as zinc and iron
58
Coenzymes
Organic molecules
Vitamins are prosecutors for many coenzyme
Vitamins must be Aquarius from diet,cells cannot make them.
59
The role of coenzymes
ADase oxidizes alcohol
Alcohol cannot be oxidized unless something else is reduced.
60
The environment affects enzyme functions
The rate at which an enzyme can bind to a substrate is called the turnover number
Each enzyme has ideal conditions that includes
Tempurature
PH
Substrate concentration
Regulatory molecules
61
Temprature
Tempurature has two effects on enzymes
Changes the rate of molecule motion
- increasing temperature-increases molecular motion and the turnover number.
- decreasing temperature decreases the molecules motion.
62
Temperature comtinued
The second change is that it causes changes in the shape of an enzyme
- temperature changes above optimum will denature the enzyme
- this changes it’s shape and it can no longer bind to the substrate and catalyze the reaction.
63
PH
In a basic enviorments- lots of OH
- the acidic side chains could donate protons which affects the charge of the side chain
In and acidic enviorment
- the basic side chain could accept protons which affects The charge of the side chain
- a neutral side chain that accepts protons would become positively charged.
- A neutral side chain that donates protons would become negatively charged.
64
Enzymes
Enzymes work together in chains of reactions known as biochemical or metabolic pathways.
> Biochemical pathways are a series of reactions in which the product of one reaction becomes the substrate of the next reaction.
65
Metabolic pathway
They are series of chemical reactions carried out by separate enzymes.
It is sequence of chemical reaction, where each reaction is controlled by a separate enzyme.
The product of one enzyme serves as the substrate for the enzyme of subsequent reaction in the metabolic pathway.
66
Enzymes
These  bio chemical pathways offer
certain advantages
1) product of the reaction can be directly delivered to the next enzyme
2) The possibility of another one to the side reaction is eliminated
3) all of the reactions can be regulated
67
Enzyme regulation
Inhibitors are molecules that bind to an enzyme to decrease enzyme activity.
Competitive inhibitor’s compete with substrates For binding to the same Active site.
Non-competitive inhibitors bind to site other than the enzymes active site
68
Competitive inhibition
Competitive inhibitor‘s closely resemble the substrate and they bind into the active site of the enzyme and block the substrate from binding.

69
enzyme regulation
Allosteric enzymes exit in either in active or inactive site
Allosteric inhibitor’s bind to Allosteric site to inactive the enzyme
70
Noncompetitive inhibitation
Non-competitive because the non-competitive inhibitor does not compete with the substrate binds to the active site
71
DNE
Deoxyribonucleic acid carries the genetic instructions used in development functioning and reproduction of all organisms and some viruse
72
RNA
Ribonucleic acid
Three types of RNA are involved in converting DNA code into polypeptides
In addition RNA may:
Act as a catalyst like enzyme
Have complex regulatory rules in cells such as regulating gene expression modifying RNA.
73
Structure
Consists of
Sugar
Nitrogenous base
Phosphate group
74
The sugars
Sugars has 5c sugars
DNA has deoxyribose
RNA has ribose
Bonds to phosphate at group 3 carbon and 5carbon
Bonds to nitrogenous base at 1 carbon
(Check diagram)
75
Nitrogenous base
DNA has 4 bases
Adenine that hydrogen bonds to thymine.
Guanine that hydrogen bonds to cytosine.
RNA 4 bases
Unicoloured replaces thymine

76
How to tell the nitrogenous bases apart
Guanine and adenine have double ring structure
Thymine and cytosine have single ring structure
They all have phosphate groups
Adenine amino group double ring
Cytosine single ring with amino group
Thymine single ring with oxygen
Guanine double ring with oxygen.
77
DNA Anti-parallel strands
Two strands are parallel battle run in opposite directions
One strand runs 5 carbon to 3 carbon other runs 3 carbon to 5 carbon.
5 carbon sugar bonds to phosphate
3 hydroxyl group on sugar
DNA can be single stranded but this is most stable when double-stranded and twisted to 3D helix. 
78
Packaging DNA
In eukaryotes DNA It’s wrapped around proteins called histones a coiled form called cremation.
Structure is further compressed by supercooling FaceTime contacted Structure forms chromosomes.
Most prokaryotes lack histones but have supercoiled forms ofDNA held together by special protein.
79
RNA structure
RNA is single-stranded
By folding it can form secondary structures that are stabilized by H bonds between nitrogenous base
80
cell membrane function
It is semi permeable which means it allows certain materials in and out of the cell
81
Cell transplant
The movement of materials in and out of cells can be passive or active.
Passive transport does not require energy
Active transport requires energy
82
Passive transport
It is the movement of materials from high to low concentration
With the concentration gradient
83
Active transport
Movement of materials from low to high concentration
Against the concentration gradient
84
Passive transport diffusion
Diffusion is the movement of small particles from high to low until equilibrium is reached
85
Passive transport osmosis
Osmosis is the diffusion of water across a selectively permeable membrane
Water will travel from high to low concentration
What are you doing in route of cells when they are placed in various solutions
Isotonic solutions - equal amount of solute in and out of the cell and the water move in and out in equal amount.
Diesel sounds does not change
86
Facilitated diffusion
Diffusion of large Molecules which must be helped through the membrane by travelling through channel proteins and carrier protein
( diagram)
87
Endocytosis
The movement of large molecules into the cell from low to high
Requires energy
Molecules bump into cell membrane
Cell membrane wraps around and engulfs particles.
Can you use a temporary vacuole for transport
88
Exocytosis
The movement of large molecules out of the cell from low to high concentration and it requires energy.
The golgi body plays a major role in the secreation of proteins and other material through exocytosis.
89
Active transport
Active transport is a carrier mediated transport where in molecules and ions Are moved against their concentration gradient across a membrane and requires energy.
90
Primary active transport
The energy is derived directly from breakdown of adenosine triphosphate or from other high energy phosphate compound.

91
Secondary active transport
The energy is derived from energy stored in the form of an ion concentration gradient between two sides of a cell membrane created originally by primary active transport.
92
Carier protein
An active transport carrier protein works differently from the carrier in facilitated diffusion because it is capable of importing energy to the transported substances to move it against the electro chemical gradient by acting as an enzyme in breaking down ATP itself
93
Primary active transport
In primary active transport energy in the ATP is required to change the affinity of the carrier proteins binding site when it is exposed and opposite sides of the plasma membrane
The carrier protein also acts as an enzyme that has ATPase activity which means it splits the terminal phosphate from an ATP molecule to yield ADP and inorganic phosphate plus free energy.
Check N a - k pump
94
Secondary active transport
This is also called coupled transport. in secondary active transport the downhillflow of of ion is linked to the uphill movement of a second solute either in the same direction as the ion oh in the opposite direction of the ion.
Check diagram
