Midterm Flashcards
1
Q
First tenet
A
All living organism are composed of one or more cells
2
Q
Second tenet
A
The cell is the basic unit of structure and organization in organisms
3
Q
Third tenet
A
All cells come from pre existing cells
4
Q
What are the two basic cell types
A
Prokaryotic and eukaryotic
5
Q
Prokaryotic nucleus
A
No true nucleus or any membrane bound organelle
6
Q
Prokaryotic cell size
A
Smaller cell (1-5um)
7
Q
Prokaryotic amount of cells
A
Always unicellular
8
Q
Prokaryotic cell division
A
Binary fission
9
Q
Prokaryotic reproduction
A
Always asexual
10
Q
Type of prokaryotic cells
A
E.coli
11
Q
Eukaryotic nucleus
A
Had a nucleus and membrane bound organelles
12
Q
Eukaryotic cell size
A
Large cell (10-30um)
13
Q
Eukaryotic amount of cells
A
Usually multicellular
14
Q
Eukaryotic cell division
A
Mitosis/meiosis
15
Q
Eukaryotic reproduction
A
Sexual or asexual
16
Q
Types of eukaryotic cells
A
Plants and animals
17
Q
Types of cells found in human body (8)
A
Muscle
Nerve
Connective tissue
Bone
Secretory
Adipose
Epithelial
Red blood cell
18
Q
Epithelial cell function
A
Form protective barrier in tissue and may be specialized to absorb or secrete compounds
19
Q
Muscle cell function
A
Are responsible for movement of the skeleton, heart and many organs. These are specialized structures and proteins that allow them to generate motion
20
Q
Nerve cell function
A
Conduct electrical signals throughout the body, control the contraction of muscles, and are responsible for senses including taste, touch, smell, sight and hearing
21
Q
Connective tissue cell function
A
Create extracellular material that holds cells together in tissue.
22
Q
Bone cell function
A
Form the bones of the skeletal system that give strength and support to the body
23
Q
Secretory cell function
A
Form glands and secrete substance ie hormones enzymes
24
Q
Adipose cell function
A
Are located throughout the body to store fat. Fat in the form of triglycerides which are released when the body is in a period of fasting
25
Red blood cell function
Are cells formed in bone morrow and released into circulation where they move and deliver oxygen throughout body
26
Eukaryotic cell structures
Plasma membrane
Nucleus
Mitochondria
Endoplasmic reticulum
Golgi apparatus
Cytoskeleton
Endosomes
Lysosome
27
What is the plasma membrane
Is like the city limit and border police. It is semi permeable phospholipid bilaterally that keeps all of the cells organelles contained and regulates what cane come in or leave
28
What is the nucleus
Is the leader of the cell, makes the law. the nucleus stores these law in the dna and protects it
29
What is the mitochondria
Are the power plants of eukaryotic. They produce energy for the cell to use in all of its processes in the form of ATP
30
What is the endoplasmic reticulum
Acts as a highway system, carrying molecules around the cell and as a factory warehouse that makes lipids and proteins and stores ions
31
What is the Golgi apparatus
Is the post office of the eukaryotic. That processes and packages proteins then sends them across the cell
32
What are endosomes, lysosomes
Some smaller membrane bound organelles contain specific proteins and enzymes.
33
What do endosomes do
Are the waste collection vehicles that sort and start breaking things down
34
What do lysosomes do
Are recycling plants that break down proteins, lipids, and nucleic acid
35
What do peroxisomes do
Deal with hazardous waste such as hydrogen peroxide
36
What is the cytoskeleton
Is the steel girdles holding building together. Actin, microtubles and filaments stabilize memodeformations
37
What are the two building blocks of a cell
Carbon and water
38
What is polarity
Polar properties of water make it an excellent solvent. This facilitates the delivery of nutrients and removal of wastes
39
What is heat capacity
The high specific heat capacity of water allows for thermoregulation by acting as a heat sink for many chemical reactions that occur within a cell
40
What is carbon
Is the building block to all life. It is small and can form up to four covalent bonds
41
Four carbon based molecules
Benzene, pyridine, cyclopentane, cyclohexane
42
What are lipids
Are the building blocks of oil and fats. They are made up of hydrocarbon chains and often insoluble in water
43
What is amphipathic
A molecule that is both hydrophilic and hydrophobic
44
What are three common lipids
Cholesterol
Phospholipids
Triglycerides
45
What is cholesterol
Regulates cell membrane fluidity and is a biological precursor for compounds such as steroid hormones, bile acids and certain vitamins
46
What are phospholipids
Are amphipathic lipids that form cell membranes. Have a hydrophilic head and a hydrophobic tail
47
What are triglycerides
Are the main component of body fat used to store energy
48
What are carbohydrates
Classified as mono, di, oligo, polysaccharides
49
What is monosaccharides
Are single carbohydrate molecules containing only carbon hydrogen and oxygen. Ie glucose
50
What is disaccharides
Are two monosaccharides bonded together connected by a glysosdic bond. Ie sucrose
51
What is oligosaccharides
Are composed of three to ten monosaccharides linked together. Ie raffinose
52
What is a polysaccharides
Are much longer chains, are even more complex, and play many important roles in the cell. Ie glycogen
53
What is nucleotides
Are the building blocks of nucleic acids like dna and rna
54
What does DNA stand for
Deoxyribonucleic acid
55
What does RNA stand for
Ribonucleic acid
56
What are amino acids
Are the building blocks of peptides and proteins
57
The carboxylic group
Can also exist as a negatively charged carboxylate
58
The r-group amino acid
Is unique to each amino acid and gives it its distinct molecular characteristics
59
Types of R-group amino acids
Hydrophobic amino acid
Charged hydrophilic amino acids
Polar amino acids
Aromatic amino acids
60
What is a hydrophobic amino acid
Also called nonpolar. Normally found in the core of the protein or interacting with fats and lipids
61
Hydrophobic: aliphatic
The R-group consist of carbon chains which can be straight, branched, or non-aromatic rings. Ie glycine, alanine valine
62
Hydrophobic: aromatic
The R-group contains an aromatic rings that has double bonds similar to benzene
63
What is charged hydrophilic amino acids
Carry a positive or negative charge. Location of charge found on the outside of proteins they interact with water. Ie lysine, arginine
64
What are polar amino acids
Can form hydrogen bonds that stabilize proteins. They are common in the outside of a protein. Ie serine, tyrosine
65
What is cysteine
Has a sulfur containing thiol that can form a covalent bond. These are significant for forming and maintaining three dimensional protein structures
66
What are aromatic amino acids
Ring structures with double bonds that have distinct properties associated with this chemical structure. They are very large
67
What are amphipathic amino acid
Having both hydrophilic and hydrophobic parts
68
What are peptides
A short chain of amino acids connected together to form peptide bonds
69
What are proteins
Made up of long chain amino acids 20 plus called polypeptides
70
what is a genome
The complete set of genetic material in an organisms aka all DNA in cell
71
What are genes
A sequence of nucleotides in DNA that determines certain characteristics
72
What is DNA held by
Phosphodiester bonds
73
What is the structure of a nucleotide
Five carbon sugar
Phosphate group
Nitrogenous base
74
What is the phosphate group
Attach to the 5 or 3 carbons
75
What is nitrogenous base
Two categories of bases: purines and pyrimidines. Attach to 1 carbon of sugar in a single nucleotide
76
What are purines
Have two rings in their structure: adenine and guanine
77
What is pyrimidines
Only have one ring in their structure:
Cytosine and thymine (DNA)
Uracil (RNA)
78
What does adenine pair with
Thymine
79
What does guanine pair with
Cytosine
80
What is a double stranded helix
DNA becomes a double stranded helix when bases comes into little contact of water creating a spinal staircase
81
What is RNA
A nucleic acid plays a critical role in synthesis of proteins
82
RNA structural differences to DNA
Nucleotides in RNA contain ribose rather than dexyribose.
RNA single stranded and is less stable then DNA
83
RNA functions and types
Messenger RNA
Transfer RNA
Ribosomal RNA
84
What is messenger RNA
Carrie’s instructions for making proteins in the cell
85
What is transfer RNA
Brings amino acids for protein synthesis during translation
86
What is ribosomal RNA
In charge of translating RNA into protein
87
What are Exons
Coding DNA contains information that is used to make protein
88
What are introns
Non-coding DNA not used to make protein
89
What is regulatory sequences
Control when a gene is turned on or used
90
Processes need for information to be converted from DNa to protein are?
Replication
Transcription
Translation
91
What is replication (DNA)
DNA is replicated before a cell divides so that both the original cell and the new daughter cells each have a complete copy of DNA (enzyme involved polymerase)
92
What is transcription
Information from a section of the DNa is transcribed into RNA to transport this information out of the nucleus for protein production (enzyme involved is RNA polymerase)
93
What is translation (RNA)
RNa is read and translated from nucleotides to amino acids to produce proteins that perform a specific function in the cell (enzyme used ribosome)
94
What are the three major stages of DNA replication
Initiation
Elongation
Termination
95
DNA: initiation of replication
- Double stranded DNA needs to be separated into single strands
- protein in binding
- DNA unwinding
-RNA Primers
96
DNA: initation of replication (protein binding
A group of proteins binds to the ORC to begin replication (most important DNA helicase)
97
DNA: initation of replication (DNA unwinding)
DNA helicase unwinds DNA into two single strands called the replication fork. This is where replication occurs
98
DNA: initation of Replication (RNA Primers)
Each single strand will act as template for synthesis for new strands
99
DNA stage two: elongation
Primers are elongated by DNA polymerase
100
DNA stage two: elongation (direction)
DNA polymerase can only add nucleotides to the 3 end of dna thus meaning it can only move along parent strand dna in a 3 to 5 direction
101
DNA stage two: elongation (catalysis)
The new phosphodiester bonds between an incoming nucleotide and existing in the backbone
102
DNA stage two: elongation (leading strand)
Runes 3 to 5 direction along parent strand
103
DNA stage two: elongation (lagging strand)
Built 5 to 3 direction running away from replication fork
104
DNA stage three: termination
A stretch of dna can’t be replicated. Causing an over hang
105
DNA stage 3: termination (overhang)
To prevent shortening of chromosomes telomeres are added which are long non coding ends of each chromosomes
106
RNA polymerase
Synthesis of RNA from dna is facilitated by this enzyme
107
RNA polymerase I
Is responsible for synthesizing most of the rRNA required for a functional risbosome
108
RNA polymerase II
Synthesizes messenger RNA
109
RNA polymerase III
Synthesizes transfer RNA as well as some other RNA molecules
110
RNA transcription three mechanisms
Guiding RNA pol II to correct strand
Unwinding DNA
Phosphorylating RNA pol II
111
Three post transcriptional RNA
5 methylguanosine cap
3 polyadenylation
Splicing
112
RNA 5 methylguanosine cap
Occurs shortly after mRNA synthesis to protect mRNA molecule from premature degradation by nucleases
113
DNA and RNA replication occurs in
Nucleus for both
114
DNA and RNA product
DNA: replication of DNA
RNA: RNA made from one or few genes
115
DNA polymerase involvement
DNA: dna polymerase
RNA: RNA poll II
116
Codons
Important to know they are three nucleotides long
117
Main components of translation
MRNA
Protein factors
TRNA
Ribosome
118
MRNA
Is delivered along with some protein from nucleus to the cytoplasm
119
Protein factors
Help the small ribosomal subunit identify the initiation site
120
tRNA
To deliver the correct amino acid to a growing peptide
121
Ribosome
Composed of large and small subunit
Small: is responsible for binding to mRNA
Large: has three important sites A P E
122
Factors that can damage DNa
UV light
Oxidation
DNA strand breaks
123
Four types of DNA mutations
Point of mutations
Insertion
Deletion
Large scale deletion, insertion, recombination
124
Point of mutation
A single nucleotide is changed resulting in one of three outcomes
Silent mutation
Missense mutation
Nonsense mutation
125
Silent mutation
Does not cause amino acid to change
126
Missense mutation
Does cause the amino acid to change
127
Nonsense mutation
Replaces an amino acid codon with a stop codon ending translation and preventing the production of the rest of the amino acid
128
Insertion mutation
An extra base pair is added to DNA which alters every amino acid produced
129
Deletion mutation
Base pair or more is removed from DNA sequence
130
Nuclear envelope
131
Nuclear pores
Allows large molecules to enter and exit the nucleus
132
Nucleoplasm
Contains nuclear nutrients and a network of filaments provides organization to the DNA
133
Chromatin
Is a complex of DNA and proteins forming highly organized fibres and is located in different defined areas of the nucleus
134
Chromosomes
Are highly condensed chromatin found in the nucleus only during cell division
135
Nucleolus
Organizes chromatin for genes that encode rRNA production site for ribosomes
136
Nuclear matrix
- helps to organize chromosomes into compartments
- helps maintain structure of nucleus
137
Function of nucleus
Protects DNA
138
DNA packaging
Helps package DNA carefully into nucleus
139
5 levels of DNA PAckaging
The DNA double helix
nucleosomes
Chromatin fibres
Chromatin looped domains
Heterochromatin
140
Nucleosomes
Known as Beads on a string
DNA wrapped twice around protein called histones shorting DNA
141
Chromatin fibre
Involves the string of nucleosomes coiled into a spiraling fibre
142
Chromatin looped domains
The 30-40um chromatin fibre made of nucleosomes is formed into loops with an average length of 300um
143
Heterchromatin
The folded looped domains formed by DNA are further compressed and folded
144
The endomembrane system consists of
Rough ER
Smooth ER
Golgi apparatus
145
Endomembrane system function
Process the transport of cargo throughout the cell
146
Exocytic pathway
The process of moving cargo out of the cell
147
Endocytic pathway
The process of moving cargo into cell
148
The endoplasmic reticulum
Is made up of organized flattened disks of the membrane called cisternae
149
Cytosol
A fluid contained by the plasma membrane of the cell
150
Rough ER
Is the site for protein translation and some protein modifications
151
Smooth ER
Does not have ribosomes on it and is responsible for lipid processing, carb metabolism and can store calcium
152
Calcium regulation
Regulates calcium ion concentration in muscle cells which is important for muscle contraction
153
Transport vesicles
Proteins that have been made in the ER are shuttled in transport vesicles to Golgi apparatus for further modifications
154
Golgi apparatus
Is involved in both protein modification and transport. Acts as post office, labels and sorts proteins and directs them to their final destination
155
Three regions of the Golgi apparatus
Cis Golgi network
Medial Golgi network
Trans Golgi network
156
Cis Golgi network
Receives proteins from the ER that have entered the endomembrane pathway
157
Medial Golgi network
Sugar groups called oligosaccarides can be added to proteins
158
Trans Golgi network
Performs the final packaging to send materials to different organelles and sorts cargo to specific destinations
159
Tran Golgi network levels
Other organelles
Retrograde transport
The lysosomes
Cargo transport
160
Trans Golgi network: other organelles
The cell needs to deliver the correct proteins to organelle
Packages these product to go to their final location
161
Trans Golgi network: retrograde transport
Some proteins that have arrived from ER contain ER retention signal
162
Trans Golgi network: the lysosome
M6P is added
163
Trans Golgi network: cargo transport
Transport of vesicles to the outside of the cell is accomplished by exocytosis
164
Endosomes
Hold content coming into the cell from the extracellular space. They help sort cargo
165
Lysosomes
Involved in waste disposal break down proteins lipids
166
Perixisomes
Break down molecules specifically those that generate hydrogen peroxide as a byproduct
167
Lumen
Is the interior space of a tubular structure
168
4 steps of translocation proteins into ER
Signal sequence
SRP binding
ribosome docking
Translocation
169
Translocation proteins ER: signal sequence
Transport of proteins into the ER begins during translation this is accomplished by the presence of signal that translated as part of the protein
170
Translocation proteins ER: SRP binding
As it emerges from the ribosome interacts with receptor. These bind to the ribosome that translating the protein
171
Translocation of proteins ER: ribosome docking
During the pause in translation the ribosome docks onto the ER membrane by the SRP interacting with an SRP receptor
172
Translocation of proteins ER: translocation
Restarts and once the proteins has translocated into the ER
173
Transmembrane domain
The translocation for transmembrane proteins recognizes a signal that is similar to the ER signal sequence
174
Enzymes involved in post translational modification
Protein disulphide
Binding protein chaperone
175
Protein disulphide
They help form disulfide bonds between the thiol group I. The side chains of the cysteines. Helps protein to fold and stabilize
176
Binding protein chaperonins
Help fold the polypeptide by binding hydrophobic patches in recently translated proteins
177
Formation of peptide bonds
Carboxylic acid group of one amino acid and the amino group of a second amino acid undergo dehydration
178
Protein structure hierarchy primary
Is a linear peptide sequence starts at amino acid terminal end of peptide and concludes at the carboxy terminus
179
Protein hierarchy secondary
Are the region of organization in the peptide sequence
180
Protein hierarchy secondary: alpha helix
Is a tight coil that forms hydrogen bonds between the backbone of every fourth amino acid
181
Protein hierarchy secondary: beta sheets
Are planes that are formed between rows of amino acids with hydrogen bonds between the backbones
182
Protein hierarchy tertiary
Is the 3D structure of a complete protein
183
Protein hierarchy quaternary
Is when multiple proteins are assembled into a complex ex hemoglobin
184
Domains
Is the basic building block of protein structure. Can be composed of 20 or more amino acids
185
What defines shape and function of protein
PH
Temperature
Ions such as calcium or magnesium
186
Two major types of modifications
Covalent mod (long lasting)
Noncovalent mod (short lived)
187
Plasma membrane
is made up of phospholipids which form double layered sheets
188
Semi permeable
Means that some molecules may cross while other cannot
189
Hydrophobic
Molecules sand small neutral molecules can freely diffuse through
190
Polar organic
Molecules ions and proteins cannot diffuse through a membrane
191
Phospholipids
Are independent entities and do not form polymer rather they are separate molecules that cluster together to form structures such as membranes
192
Phospholipids are composed of four major components
Head group
Phosphate group
Glycerol
Two fatty acid tails
193
Phospholipids: head group
Attached to phosphate group and its chemical properties determine where the phospholipid ends up in the cell
194
Phospholipids: phosphate group
The hydrophilic charged component of the phospholipids
195
Phospholipid: glycerol
Is a three carbon chain with three hydroxyl groups it acts as the backbone of the phospholipid
196
Phospholipids: fatty acid tail
Two long hydrocarbon chains which can vary in composition and bond. Attach to the glycerol backbone
197
The six major types of phospholipid head groups
Polar: phosphatidyl-inositol (PI), phosphatidyl-glycerol (PG)
Cardiolipin (CL)
Charged: phosphatidyl-serine (PS), phosphatidyl-ethanolamine (PE)
Phosphatidyl-choline (PC)
198
Other classes of lipids
Cholesterol
Glycolipids
Sphingonyelin
199
Cholesterol
Major membrane component in tissues. Key component has hydroxyl group on one of its rings
200
Glycolipids
Are also common in membranes and have sugar carbohydrate group attached to the lipid. Often involved in cell to cell signalling
201
Sphingonyelin
Another common component in cell membranes. Found wrapping around axons of nerve cells
202
Sphingolipids
Consists of phosphcholine head group, phosphate group, sphinosine and a fatty acid
203
Phospholipids clusters
Spontaneously to maximize hydrophobic and hydrophilic interactions can reform easily and does not require high amounts of energy
204
Four major types of phospholipid cluster
Micelles
Liposomes
Monolayer
Bilayer
205
Micelles and liposomes
Surrounded by polar water phospholipids will form either droplets with fatty acid tail in center (micelles) or tight bolsters with hollow middle (liposomes)
206
Monolayer
At the boundary of water and atmosphere phospholipids will form a single layer with the polar head groups pointed down into the polar h2o
207
Bilayer
In cells phospholipids form bilateral with the polar head groups pointed out towards the aqueous environment inside and outside the cell
208
Cytoplasmic leaflets
Leaflets facing the cytoplasm
209
Exoplasmic leaflet
Leaflets facing the exterior of the cell
210
Types of transporters
Floppases
Flippases
Scrambalases
211
Floppases
Keep most PC, sphingomyelin and cholesterol in the exoplasmic leaflet (to flop out)
212
Flippases
Keep most PS, PE, PI in the cytosolic leaflet (to flip in)
213
Scramblases
Briefly disrupt membrane asymmetry by randomizing phospholipids
214
Gradients
As an increase or decrease of the magnitude of property from one point to another
215
Osmotic gradients
Difference in concentration of molecules between one side and other side leads to osmotic pressure
216
Aquaporins
Are channels that have a hydrophilic interior to allow water to move through the plasma membrane
217
Three classifications of tonicity
Hypertonicity
Isotonicity
Hypotonicity
218
Hypertonicity
Solution has greater amounts of solute outside of the cell than inside. Causing water to flow out of the cell. This causes the cell to lose volume
219
Isotonicity
Solution has equal amounts of solute inside and outside of the cell. The ideal state for a cell
220
Hypotonicity
Solution has lower amounts of solute outside the cell than inside. Causing water to flow in. This makes the cell swell
221
Fluid mosaic
Proteins reach membrane
222
Types types of revised fluid mosaic model
Membrane constituents
Hydrophilic groups
223
Fluid mosaic: membrane constituents
Phospholipids proteins can join together to form complexes in the membrane
224
Fluid mosaic hydrophilic groups
Hydrophilic head groups of phospholipids can interact with hydrophilic portions of the membrane proteins.
225
Lipid raft
Is a cluster of membrane proteins, phospholipids and other membrane constituents forming distinct patches that are chemically and physically distinct from the surrounding membrane
226
Factors affecting membrane fluidity
Temperature
Lipid content
Cholesterol content
Protein content
227
Membrane fluidity: temperature
Increase the motion in the membrane increase making it more flexible. Cooler temps cause the membrane to become more rigid
228
Membrane fluidity: lipid content
The length of lipid chains influences the rate of movement of the plasma membrane. Shorter lipids move more compared to longer chains
229
Membrane fluidity: cholesterol content
Is rigid bulky and hydrophobic and thus acts as a spacer in lower concentrations making a membrane more fluid. Higher concentrations will make the membrane more rigid and reduce membrane fluidity
230
Membrane content: protein content
Some membranes in the cell are very rich in protein and therefore have less movement in the membrane
231
Parts of membrane protein
Signalling molecules
Intergins
Receptors
Channels and transporters
Anchors and junctions
232
Signalling molecules
Include proteins involved in cell communication
233
Integrins
Are membrane bound proteins that facilitate cell adhesion and cytoskeleton movement
234
Receptors
On the surface of cells can facilitate endo or exocytosis or be used in cell signalling
235
Channels and transporters
Moving material across the membrane
236
Anchors and junctions
These proteins help cells move and attach to other cells and extracellular matrix
237
Two categories of membrane transport
Passive and active
238
Passive transport
Is movement of molecules across a membrane down their concentration gradient which does not require energy. Ie, simple diffusion or facilitated diffusion
239
Channel mediated transport
Form pores allowing water and small charged molecules such as ions to pass through the hydrophobic membrane. Act as gates that open and close
240
Carrier proteins
Undergo a conformational change to allow their cargo to pass from one side of the membrane to the other
241
Active transport
Requires energy to move molecules across the membrane against their concentration gradient. Ie pump protein ATP used
242
Direct active transporter
Antiporter pump. The pump directly uses ATP to create NA and K gradients
243
Indirect active transport
Na/glucose supporter. It uses Na to create a glucose gradient (ATP no required)
244
Two biochemical reactions
Catabolism
Anabolism
245
Catabolism
Is the breakdown of cellular macromolecules with respect to cellular energy. Releases stored energy
246
Anabolism
Is the production of cellular macromolecules. Consume the ATP produced by catabolism as small molecules are built into macromolecules (requires energy)
247
What is ATP
Adenosine triphosphate is the primary energy source for cellular processes composed of adenine molecule, a ribose sugar and chain of three phosphates
248
What is ADP
Adenosine diphosphate, when the third phosphate is removed from ATP
249
What is GDP
Guanosine triphospahte identical to ATP except the adenosine is replaced with guanosine
250
Other high energy molecules
NAD
fAD
251
What is NAD
Nicotinamide adenine dinucleotide is converted to high energy form by the addition of an hydrogen ion and two electrons
252
What is FAD
Is converted to high energy form by addition of two hydrogen ions and two electrons
253
Cristae
Inner membrane appears to be closed in on itself to form structures
254
Matrix
Inside the mitochondria is called the matrix this is where macromolecules are converted into small high energy compounds
255
Three primary sources of energy
Carbs
Fats
Proteins
256
Carbs
Stored as mainly glycogen in muscles and the liver. Muscle glycogen is more readily available for actively working muscle
257
Fats
Stored as tricyglycerols throughout the body they must be broken down to release free fatty acids that need transported into the cells that need energy
258
Proteins
Are stored in skeletal muscle which is why there is muscle wasting if the body needs to use proteins as an energy source
259
Carbs three major classes
Monosaccharides
Disaccharide
Polysaccharide
260
Monosaccharides
One sugar are most commonly consumed in the form of glucose
261
Disaccharide
More complex consist of two mono bonded by alpha and beta glycosidic linkage
262
Polysaccharide
Even more complex which are much longer chains of mono
263
Brains main energy source
Glucose and ketones
264
Heart main energy source
Fatty acids and some ketones
265
Skeletal muscle main energy source
Glucose
Fatty acids
Ketones
