Biochemistry Flashcards
(129 cards)
1
Q
Define “Organic Molecules”
A
Organic molecules are carbon based and are often bonded to Carbon or Hydrogen atoms and/or are made by living beings
2
Q
Explain Carbon and its general structure
A
It can form up to 4 covalent bonds that can form geometric structures that serve as the backbone for all biological molecules
Structures such as straight chains, branches or rings
3
Q
What is CHNOPS?
A
99% C, H N and O with 1% Phosphate and S
4
Q
What are isomers?
A
molecules with the same formula but different arrangements
5
Q
What is the formula for Glucose, Fructose and Galactose?
A
C6H12O6
6
Q
Why is the 3D shape of a molecule so important?
A
- Determines function and behaviour of molecule
7
Q
Define “Molecular Formula”
A
What amount of each atom is present in each compound
8
Q
Define “Structural Formula”
A
shows how each atom is bonded
9
Q
What are Functional Groups?
A
atoms or groups of atoms attached to molecules that give the molecule certain properties, usually containing O, N, P
Certain groups are associated with chemical properties they give to molecules within that group
10
Q
Name the properties of hydroxyl and give an example
A
- polar
- -OH
- found in carbohydrates, proteins, nucleic acids and lipids
11
Q
Name the properties of carbonyl and give an example
A
- such as ketone and aldehydes
- polar
- found in carbohydrates and nucleic acids
12
Q
Name the properties of carboxyl and give an example
A
- acidic
- polar
- found in proteins and lipids
13
Q
Name the properties of Amino and give an example
A
- basic
- polar
- found in proteins, nucleic acids
14
Q
Name the properties of Sulphahydryl and give an example
A
- slightly polar
- found in proteins
15
Q
Name the properties of phosphate and give an example
A
- polar
- negative charge
- found in nucleic acids
16
Q
What is methyl?
A
- CH3
17
Q
Draw all of the functional groups
A
check notes
18
Q
What is a condensation reaction?
A
- aka dehydration synthesis
- anabolic reaction
- makes polymers by forming covalent bonds between two molecules and produces water as a result
- H is removed from one group and HO from another
19
Q
What is a hydrolysis reaction?
A
- catabolic reaction
- breaks down polymers by breaking covalent bonds between them after ADDING water to the reaction
- H from water is added to one OH group
20
Q
Describe Alkalosis and Acidosis
A
Alkalosis: when blood pH gets too high
Acidosis: when blood pH gets too low
21
Q
Describe a redox reaction
A
- oxidation reaction that loses electrons and reduction reaction that gains electrons at the same time to transfer electrons from one reactant to the other
22
Q
What are carbohydrates?
A
- contain C, H and O in a 1:2:1 ratio
- sugars and starches
- high amount of hydroxyl groups and some carbonyl
- most are polar and water-soluble
23
Q
What is the main functions of carbs?
A
- to store short term energy that is easily accessible to the human body as it contains bonds recognized and broken down by enzymes
24
Q
What are monosaccharides?
A
- carbs made of 3-7 C atoms in a single carbon based monomer structure
25
What is glucose?
- monosaccharide found in blood sugar
- first sugar body uses for energy
- there is alpha glucose and beta glucose
26
What is fructose?
-sugar found in fruits
- slightly sweeter
27
What is galactose?
- sugar found in milk
28
Why is shape important for monosaccharides?
- arrangement of H atoms and hydroxyls differ and are treated differently by the body, such as why fructose is sweeter than glucose
29
Draw: Alpha and Beta Glucose, Fructose and Galactose
see notes
30
What are disaccharides?
- carbs made of two monosaccharides joined by a glycosidic linkage
31
Explain a glycosidic linkage, and draw an example
- link formed between two monosaccharides by koining two hydroxyl groups in condensation reaction
- see notes for drawing
32
Give three examples of disaccharides and what they are made of
1. Sucrose: Glucose and Fructose
2. Maltose: Glucose and Glucose
3. Lactose: Glucose and Galactose
33
What are polysaccharides?
- carb polymers made up of many monosaccharides joined by glycosidic linkages
34
What is the linkage between carbs?
glycosidic linkages
35
Give three examples of monosaccharides
1. Glucose
2. Fructose
3. Galactose
36
Give four examples of polysaccharides and their function
1. Starch: storage for plants
2.Glycogen: storage for animals
3. Cellulose: structural support
4. Chitin: structural support
37
What are the subgroups of starch?
1. Amylose and Amylopectin
38
What is amylose?
- linear unbranched simple starch with alpha 1,4 glycosidic linkages
- hard to digest and insoluble
39
What is amylopectin?
- complex starch
- branches made of alpha 1,4 and 1,6 glycosidic linkages
- soluble and easy to digest
40
What is glycogen?
- made of highly branched chains of glucose
- many alpha 1,4 and 1,6 glycosidic linkages
-replenished by eating
41
What is cellulose?
- provides structure for plant cell walls
- made of beta glucose and beta 1,4 linkages
- humans cannot digest
- used in lumber and cotton/paper manufacturing
42
What is chitin?
- modified cellulose w added amine
- found in fungi cell walls and exoskeletons of insects/crusteaceans
- insoluble and not easily digested
- made of beta glycosidic linkages
43
What are lipids?
- made of C, H and O
- more C and H than O, therefore nonpolar
- soluble in oils and not water
44
Explain hydrophobic
- repelled and non soluble in water
45
The main functions of lipids are:
- long term energy storage bc of hydrocarbons
- less accessible energy
- provide insulation
- cushions organs
- waterproofing in animals
- makes up cell membrane
- communicators for chemical signals
46
What are the monomers of lipids?
- Glycerol
- Fatty Acids
47
What is glycerol?
- made of hydrocarbons and hydroxyls
48
What are fatty acids?
- HC chain ending in carboxyl
* presence of double bonds affects shape and properties
49
What is the difference between saturated and unsaturated fats?
Saturated: no double bonds, straight chains, solid at room temp.
Unsaturated: 1+ double bonds, bent chains,liquid at room temp.
50
What is the difference between cis fats and trans fats?
- Both are unsaturated
Cis: cis double bonds and bent
Trans: trans double bonds and bent (dangerous)
51
What are triglycerides:
- lipid polymers made of 1 glycerol and 3 fatty acids
- hydroxyl on glycerol bonds w carboxyl in fatty acid
52
What is an esther linkage?
- bonds in lipids where hydroxyl on one group matches with carboxyl on another in condensation reaction
53
What are phospholipids?
- composed of R group bonded to glycerol to phosphate group to two fatty acids
- hydrophillic, polar head
- hydrophobic tail, non polar
- used in cell membranes in lipid bilayer
54
What are steroids?
- made of 4 attached C rings
- mainly hormones
55
What is cholesterol?
- steroid found in animal blood and cell membranes
56
What are waxes?
- made of long C based chains
- solid at room temp
57
Name all the types of lipids learned
1. glycerol
2. fatty acids
3. triglycerides
4. steroids
5. waxes
58
What are proteins?
- made of amino acid monomers
- very diverse in structure and function
59
The main functions of proteins are:
- catalyzing reactions like enzymes
- providing structural support
- transporting substances in body or to membrane
- enables organisms to move (contractile)
- regulates cellullar processes like hormones
- defensive measures
- receptors that respond to chemical stimuli
60
What are the monomers of proteins?
Amino acids
61
What are amino acids?
- composed of central C atom bonded to H atom, amino group and carboxyl and R group that determines its function
- hydrophillic
- or hydrophobic
- acidic with a negative charge
- basic with a positive charge
- all are somewhat polar
62
How many amino acids are there?
20
63
How many essential amino acids are there? Why are they essential?
8, because they need to be consumed
64
what bond joins amino acids?
peptide bonds
65
Describe a peptide bond
- formed w carboxyl group and amino group on two amino acids in condensation reaction
66
What are polypeptides
protein polymers of amino acids
67
What are the 4 levels of protein structure?
1. primary - specific amino acids join together to form polypeptides
2.Secondary - polypeptides lengthen to for alpha helix coils or beta pleated sheets
3.Tertiary - polypeptides fold w extra bonds
4. Quarternary - form from multiple polypeptides to form a larger functional protein
68
What is denaturation?
when a proteins 3D shape changes due to tempor harsh chem conditions
cannot carry out its original function
69
What are the monomers of nucleic acids?
made of nucleotides
70
Name the two types of nucleic acids
1. DNA (deoxyribonucleic acid)
2. RNA (ribonucleic acid)
71
Nucleotides definition?
- molecules made of sugar bonded to a phosphate group and nitrogen base
72
What kind of sugar does RNA and DNA have?
RNA : ribose sugar (w OH)
DNA: deoxyribose sugar (no OH, yes H)
73
What are the different nitrogenous bases?
For DNA: adenine, thymine, cytosine, guanine
For RNA: uracil
74
Purines vs Pyrimidines
Purines: two C backbones (A and G)
Pyrimidines: one C backbone (C, T, U)
75
What is a nucleic acid strand?
- polymer of nucleotides with a backbone of alternating phosphates and sugars
76
What bonds nucleotides? Explain.
- phosphodiester bonds between phosphate group on one and hydroxyl group on another in condensation reaction
77
What are enzymes?
- protein catalysts that speed up reactions with a lower activation energy. Very specific, and some reactions are reversible. Usually with the -ase suffix
78
Define substrate:
- reactants in enzymatic reaction
79
Describe the process of an enzyme reaction
1. enzyme bonds to substrate to form enzyme-substrate complex
2. reaction occurs and substrates either form one product or split into two (condensation and hydrolysis)
3.Products are released and enzyme is available again
80
Induced Fit Hypothesis vs Lock and Key
Induced Fit: functional groups on substrate interact with that of the enzyme to change the shape of the active site to an induced fit for better grip
Lock and Key: old suggestion that enzymes and substrates match perfectly and active site does not change, but fails to account for substrates and enzymes that do not match
81
What is the active site?
the site the substrate binds to
82
What is the allosteric site?
the site that other molecules can bind to so to regulate enzyme acitivty
83
Explain competitive inhibition
- inhibitors compete with substrate for the active site. If substrate is more concentrated then it can be reversed
84
What is an inhibitor for enzymes?
molecules that restrict the action of an enzyme
85
What is non competitive inhibition?
- inhibitors attach to allosteric site ti change shape of enzyme so that it no longer has affinity for the substrate
86
Explain feedback inhibition
- controls enzyme production
- uses product formed at later stage of enzyme chain to allosterically inhibit earlier enzyme to reduce the production of a final product
- when all products are used up, the enzyme becomes active again
87
What happens to an enzyme when the temperature increases?
- more reactions occur
- of too high the enzymes become denatured which changes the shape of the active site
88
What happens to an enzyme in a period of high pH?
- denatures
89
What happens as enzyme concentration increases?
- rate of reactions increase because there are enough enzymes to continually produce reactions with the substrates
90
What happens as substrate concentration increases?
- rate of reactions will increase and then plateau bc there is a limited amount of enzymes that can only work so fast
91
What makes a eukaryote different from a prokaryote?
- have DNA within a membrane bound nucleus
- cell membrane made of a phospholipid bilayer
- cytoplasm suspending all interior cell objects incell
92
What are the organelles unique to animal cells and plant cells?
Animal: lysosomes, centrioles
Plants: cell wall, granum, chloroplasts, central vacuole
93
Describe the nucleus (6)
- contains DNA
- double membrane called nuclear envelope
- pores that form openings to allow passage of certain materials
- nucleoplasm that is the thick fluid filling the nucleus
- nucleolus that is full of RNA, protein and chromatin
- nuclear matrix that is a network of supporting protein fibres
94
Describe the ER (3)
- network of connected membranes that carry materials throughout cytoplasm
- Rough ER: ribosomes attached to modify proteins and synthesize new ones
- Smooth ER: no ribosomes attached but float, contains enzymes that synthesize carbs, lipids and hormones
95
Describe the golgi apparatus (6)
- made of membranous sacs piled on top of each other
- in plants helps with making cell walls
- collects and modifies packages to be distributed
- produces lysosomes
- molecules come in vesicles that fuse to golgi membrane to be modified
- then pinched off in new vesicle and leaves
96
Describe lysosomes: (3)
- vesicle in animal cells that have digestive enzymes
-catalyze hydrolysis reactions to break down food, old cell parts, dead cells/bacteria
-may also kill cell when too old
97
Describe Chloroplasts (6)
- large green structures in plants to store solar energy using photosynthesis to produce glucose
- double membrane
- thykaloid: disks with chlorophyll
- stroma: liquid
- granum: stacks of thykaloid
- came from photosynthetic bacteria
98
Describe mitochondria (5)
- double membraned red organelle
- came from bacteria
- smoother outer and cristae (greatly folded interior)
- own DNA
- breaks down organic fuel molecules into useable cell energy (cellular respiration) to release ATP
99
Describe Cytoplasm (3)
- viscous fluid containing organelles
- interconnected fibres
- cytosol (fluid)
- organelles outside of nucleus and storage substances
100
What are vacuoles?
membrane bound storage sacs that store
larger in plants
101
Describe the cell wall
- made of cellulose/chitin
- surround plasma membrane
102
what are vesicles?
membrane enclosed sacs that are used for transport and storage
103
What are cilia and flagella?
Cilia: short,hair like protrusions used to move substances outside human cells
Flagella: whip like extensions found in sperm cells
104
Describe the cytoskeleton:
made of interconnected filaments as a mechanical support that anchors organelles and helpmove substances
105
What is the cell membrane?
- made of phospholipid bilayer with embedded proteins
- is fluid and flexible
- regulates passage of materials in and out of cell
106
What are integral or embedded proteins?
- embedded through membrane to move materials in and out of cell
107
What are peripheral proteins?
stick out of the inside layer and connect to the cytoskeleton
108
what are glycoproteins?
protein and carb that stick out of outside layer and allow cells to recognize each other
109
What are glycolipids?
carb and lipid that provide stability and mobility by reacting to the temperatire
110
what are lipoproteins?
- like cholesterol that keep membrane together at varying temperatures
111
what is passive transport?
transport of molecules across concentration gradient without energy
112
what is simple diffusion?
net movement of molecules from across concentration gradient but only for molecules small enough that can pass straight through membrane
113
what is hypertonic?
concentrated solution in two
114
what is hypotonic?
less concentrated solution in two
115
what is isotonic
when both solutions are equal
116
what is facilitated diffusion?
- transport of molecules across concentration gradient by using membrane proteins for bigger molecules or ions
117
explain carrier mediated diffusion
uses carrier proteins that bind to larger molecule and change their shape to accomodate them
118
explain channel mediated diffusion
uses channel proteins to allow specific smaller ions to pass through. Some remain open and others are gated
119
What is active transport?
transportation of molecules against concentration gradient with the use of energy
120
what is primary active transport?
using ATP energy to pump molecules from one side of the membrane to another
121
what is a uniport and cotransport
uniport - pumps one kind of molecule
cotransport - pumps two or more kinds of molecules
122
explain the sodium potassium pump (3)
- sodium binds to the ion pump
- ATP also binds to it and ADP is released while phosphate remains bound
- changes the shape of the pump so sodium is released outside
potassium ions bind to the pump that releases the phosphate that releases the potassium and returns to its original form
123
What is secondary transport?
using second carrier protein after setting up concentration gradient to allow bigger molecules to be transported into the cell
124
Explain antiports and symports
antiports: move molecules in the opposite direction
symports: move molecules in the same direction
125
explain the proton/glucose/sucrose pump (2)
- uses ion pump to active transport protons against the gradient
- another protein, a proton/sucrose/glucose symporter uses the proton gradient to transport sucrose against gradient into the cell, using the electrical energy of the proton concentration to do so
126
when is bulk transport used?
used when molecules are too big or polar to go through transports
127
what is endocytosis?
when membrane folds inwards to create vesicles
128
what are the three types of endocytosis?
1. phagocytosis: cell eats large particles
2. Pinocytosis: cell drinks large amounts of dissolved substances
3. Receptor mediated endocytosis: receptor proteins bind with specific molecules using energy
129
what is exocytosis?
when the vesicles with the particles fuse with the membrane to expel them using energy
