Lecture Exam 1 Flashcards
1
Q
Anatomy
A
Structure, how things look
2
Q
Levels of Anatomy
A
- Gross Anatomy
2. Microscopic Anatomy
3
Q
Gross Anatomy
A
The level of anatomy that you can see with your eyes
4
Q
Example of Gross Anatomy
A
Cadaver labs
5
Q
Microscopic Anatomy
A
Below the level of what you can see with your eyes
6
Q
Examples of Microscopic Anatomy
A
- Cytology: Study of cells
2. Histology: Study of tissues
7
Q
What is cytology used for
A
Pathologists use cytology to tell if something looks normal or abnormal
8
Q
Physiology
A
Function, what it does
9
Q
What determines the other?
A
The Anatomy determines the Physiology
- Structure determines the function
- This rule holds true at all levels of Anatomy
10
Q
Hierarchy of Life
A
- Molecular/Chemical Level
- Cellular Level
- Tissue Level
- Organ Level
- Organ System
- Organism
11
Q
Example of Molecular/Chemical Level
A
Atoms
12
Q
Cellular level
A
Molecules that are formed together
13
Q
Example of tissue level
A
Histology
14
Q
Tissue Types
A
- Epithelial (Found in skin)
- Muscle
- Connective
- Neural
15
Q
Organ level
A
Multiple tissues that come together
16
Q
Example of organ level
A
Heart
17
Q
How many organ systems do we have
A
11
18
Q
Example of organ system
A
Digestive system
19
Q
Example of organism
A
Humans
20
Q
What is the function of the organism
A
To maintain homeostasis
21
Q
Homeostasis
A
Having a stable internal environtment
22
Q
Things to keep in homeostasis
A
- Body temperature
- pH of body and blood
- Blood pressure
- Heart rate
- Respiratory rate
- Water
- Blood sugar
- Sodium
- Potassium
23
Q
What would happen if you took your temperature every morning for a month
A
It would have a wavy line on a graph because it changes all the time
24
Q
Static equilibrium
A
If your body temperature stayed the same
25
Dynamic equilibrium
Not the same everyday (changes). There is a range that is accepted
26
Why do you shiver?
Muscle contractions heat you up
27
Ways to Maintain Homeostasis
1. Autoregulation
| 2. Extrinsic regulation
28
Autoregulation
Regulation without help
29
Examples of autoregulation
Stomach
- Food puts off homeostasis, so it undergoes homeostasis to digest it
Running
- Blood to the heart increases by itself
30
Extrinsic regulation
Regulation with help
31
Where does the help for extrinsic regulation usually come from
Neural and endocrine systems
32
Types of Extrinsic Regulation
1. Feed-forward
| 2. Feed-back
33
Feed-forward
The ability to predict a change in homeostasis and begin to prepare for it before it happens
34
Examples of feed-forward
Your hungry and walk past a restaurant, your stomach growls, then it makes acid and enzymes to prepare for food
Runners that run at the same time everyday have bodies that get ready to run by increasing respiratory rate and heart rate
35
Types of Feedback (Loops)
1. Positive feedback loop
| 2. Negative feedback loop
36
Positive feedback loop
Body's response to stimulus is to exaggerate that stimulus; Used in situations where the only way to get back to homeostasis is to push through as fast as possible
37
Examples of positive feedback loops
Low body temperature.
Body's response is to make it lower
Labor and Delivery
- Stimulus is cervical stretch
- Body responds by making oxytocin (by the hypothalamus)
- Oxytocin causes cervix to stretch
- Pitocin (being induced) speeds up positive feedback loop; oxytocin
38
Negative feedback loop
Body's response to a stimulus is to revert the stimulus; The most important/most common type of regulation
39
What is the body's first response to a stimulus
Recognizing the stimulus
40
Receptors
Recognizes a stimulus and sends information to the integration center
41
Integration center
(The brain, usually) Takes in information and determines if a response is necessary; If a response is necessary it sends information to the effector
42
Effector
Acts on the stimulus (exaggerates or counteracts)
43
Types of macromolecules
1. Proteins
2. Lipids
3. Carbohydrates
4. Nucleic acids
44
Macromolecules
Organic; which means that it has carbon
45
What looks just like carbon
Silicon
46
What is unique about carbon?
The carbon bonds can twist and go from something long and linear and make them into rings
47
Macromolecules are
Polymers
48
Polymers
Big structures that are made from smaller individual units
49
Monomer
Individual units that make a polymer
50
What is the monomer that is used to make proteins?
Amino acids
51
How many amino acids are in our body?
At least 20
52
What makes amino acids different from each other?
Different R group
53
Pieces of an Amino Acids:
1. Amino group
2. Central carbon
3. Carboxyl group
4. R group (variable side chain of one or more atoms)
54
What is dependent on the R group
The chemical properties of an amino acid
55
How do you link 2 amino acids?
By freeing up a bond on both amino acids and then linking the carboxyl group to the amino group
56
Every atom has a limited
Amount of bonds it can make
57
Peptide bond
A strong covalent/chemical bond that links amino acids by linking a carboxyl and amino group
58
What does the digestive system do with peptide bonds?
It breaks it down so that we can absorb it
59
Dehydration synthesis
When the amino acid loses a molecule of water to make a peptide bond
60
Hydrolysis
The opposite of dehydration synthesis; When you add a molecule of water to break down a peptide bond
61
Protein Structures:
1. Primary structure
2. Secondary structure
3. Tertiary structure
4. Quaternary structure
62
Primary structure
Chain of amino acids that are all linked together by peptide bonds that is not functional
63
What must happen for a protein to be functional
It must turn into a 3D structure
64
Secondary structure can either be in the form of:
1. Alpha-helix
| 2. Beta-sheets
65
What is the driving force of the secondary structures?
The formation of hydrogen bonds; which are weak bonds
66
Secondary structures can be a
Combination of alpha-helix and beta-sheet structures
67
Hydrophobic interactions
The process that makes tertiary structures because the hydrophobic amino acids coil together and hydrophilic amino acids go towards the water on the outside; this is now a functional protein
68
Quaternary structure
Two or more tertiary structures that have come together
69
A protein is only functional if
It folds into the correct shape
70
Example of mutation of protein strucuture
Sickle cell anemia: An inherited mutation of hemoglobin where one amino acid is changed. This messes with the hydrogen bonds and the structure/shape
71
Catalyst
Anything that speeds up a chemical reaction but is not used up in the reaction
72
Activation energy
Energy that is needed to get a chemical reaction moving
73
Example of activation energy
Stirring sugar in water
74
Enzymes
Protein catalysts that our body uses that can be reused over and over
75
What is the function of enzymes
To make chemical reactions happen fast enough to maintain life
76
Process of an enzyme:
1. Substrates bind to active sites on enzyme
2. Substrates are held together and the enzyme bonds them to promote a product being made
3. Product leaves and the process can happen again because the enzyme can be reused
77
Active site
Pockets that are formed from the what that the protein forms
78
What do enzymes do
Lower the amount of activation energy required
79
Factors that influence enzyme activity
1. pH
| 2. Temperature
80
Every enzyme has an...
Optimal temperature
81
When do enzymes not work as well
1. Colder temperature
| 2. Hotter temperature
82
What happens to enzymes in colder temperatures
They slow down
83
What happens to enzymes in hotter temperature
It denatures
84
Denature
The 3D structure breaks down and it reverts to its primary structure
85
What happens when an enzyme denatures
The hydrophobic amino acids go into the water and are unprotected
86
Example of denature of a protein/enzyme
Eggs: When they are cooked, the protein in them breaks down and it turns from clear to white
87
Salivary amylase
An enzyme that degrades carbohydrates; found in saliva; works best as around pH 7, when food is swallowed it doesn't work well
88
Pepsin
An enzyme in the function that has an optimal pH of about 2; shows that enzymes need a specific environment
89
2 ways a drug can block an enzyme
1. Competitive inhibition
| 2. Non-competitive inhibitions
90
Competitive inhibition
Drug fits into the active site of enzyme so that the substrate cannot bind to the active site
- Whoever "wins" depends on whichever there is more of (competing for enzyme active spot)
91
Non-competitive inhibitions
Drug binds to other part of enzyme which causes the enzymes active site to change shape, blocking substrate. Does not matter how much substrate/drug there is
92
What does homeostasis do for enzymes
It creates the perfect environment for the enzymes
93
What is the inside of the plasma membrane
Cytoplasm
94
What is the outside of the plasma membrane called
Extracellular part
95
What separates the outside and inside region
The plasma membrane
96
Importance of the plasma membrane
1. Gives physical isolation
| 2. Provides a chemical boundary
97
How does the membrane help with the internal conditions of the cell
It establishes conditions within the cell that are optimal for metabolism
98
What is the main function of the plasma membrane
It is the ultimate gatekeeper, it determines what gets in and out of the cell
99
What are the major structures of the plasma membrane
1. Phospholipids
2. Proteins
3. Cholesterol
100
Major parts of phospholipids
1. Lipid tails/fatty acid chain/hydrocarbon chain
2. Glycerol (tails are attached to this)
3. Phosphate group
101
Hydrocarbon chain
Means it is made of carbon linked together and hydrogens that soak up the electron
102
Most lipids are
Hydrophobic
103
Phospholipids are
Amphipathic
104
Amphipathic
Parts of the molecule are hydrophobic and parts are hydrophilic
105
Three ways phospholipids organize
1. Hydrophilic heads on water surface, tails sticking out
2. Circle with hydrophilic heads on the outside, tails are protected on the inside
3. Bilayer
106
Bilayer
The plasma membrane is a phospholipid bilayer
107
What molecules pass through the plasma membrane freely
Hydrophobic
108
Two classes of proteins
1. Integral protein: Spans the entire plasma membrane bilayer
2. Peripheral protein: On the inside, does not span the lipid bilayer
109
What is the importance of proteins in the plasma membrane?
They facilitate membrane transport, the hydrophilic molecules move through these protein channels
110
The plasma membrane is
Fluid, or always moving
111
Fluid-mosaic model
Describes the moving plasma membrane
112
What is the purpose of cholesterol?
To control the fluidity or movement of the plasma membrane
113
How things move in and out of the cell
1. Simple diffusion
| 2. Facilitated diffusion
114
What do you need for simple diffusion to occur?
A concentration gradient
115
Concentration gradient
Different amounts of concentration
| - Things always move down the gradient, from high to low
116
Brownian motion
Things are always moving, making things collide and bounce off of each other, causing diffusion
117
What molecules move through the plasma membrane through simple diffusion
Small, hydrophobic molecules
118
What molecules use facilitated diffusion
Large, charged molecules because they are hydrophilic
119
Aquaporins
Pores that move water through facilitators back and forth across the plasma membrane
120
Osmosis
Movement of water across a selectively permeable membrane
121
Osmotic pressure
The higher the solute concentration, the higher the osmotic pressure. The side with the more solute has osmotic pressure. This describes the amount of pull that a solution has on water
122
Example of osmotic pressure
- High osmotic pressure is needed by kidneys to pull water out of urine
- Small intestine pulls water out of food waste, so it needs high osmotic pressure
123
Tonicity
Describes the effect that a solution has on a cell
124
Isotonic
Describes a solution that has solute that matches the inside. Water moves in and out for every water molecule that goes out, another goes in, creating equilibrium
125
Hypotonic
Less solute in the solution than inside the cell, or more solute inside the cell than the outside (it is plump)
126
Example of something hypotonic
Water
127
Hypertonic
More solute outside the cell than inside
128
Active transport
Moves things against the concentration gradient, from low to high; requires energy because it is not "natural"
129
Sodium-potassium exchange pump
There is more sodium outside than inside the cell, and more potassium inside than outside; They are moved against the concentration gradient using ATP
130
Secondary Active Transport
The concentration gradient of one substance provides the driving force needed to give the second substance a free ride
131
Glucose-sodium transporter
There is more glucose inside the cell than outside, so to get glucose inside the cell it gets a free ride from the concentration gradient of sodium that is coming in; uses no energy
132
What will happen to sodium over time if it only uses the glucose-sodium transporter?
It will reach equilibrium and stop moving down its gradient and stop glucose coming into the cell
133
How does sodium not reach equilibrium?
It uses both the sodium-potassium pump and the glucose-sodium transporter
134
Why is it called the secondary active transport?
Because it happens after the sodium-potassium pump and is dependent on it
135
How many transporters do we have?
A limited amount, making there be a limit to the rate of transport that can occur
136
As the concentration gradient gets larger (ex. More sodium on one side)
The rate of transport gets faster
137
Why does the rate of transport stop getting faster?
Because we have a limited number of transporters and they are all being used
138
What happens to blood that goes into the kidney tubules
Blood goes into kidney tubules, then waste is removed and urine is produced. Good things go into the tubules, like glucose, but you don't want it to go into your urine, so the glucose transporters take out the glucose before it reaches the end and turns into urine
139
Vesicular transport
Materials are moved in or out of the cell using vesicles
140
Types of vesicular transport
1. Endocytosis
| 2. Exocytosis
141
Endocytosis
Membrane makes a "bud" and pulls something in after it pinches off into the cell
142
Types of endocytosis
1. Pinocytosis
2. Phagocytosis
3. Receptor mediated
143
Pinocytosis
Constantly randomly testing fluid from the environment that can be useful or useless
144
Phagocytosis
Pulls in specific things by reaching out and capturing things from the environment
145
Receptor mediated
Extremely specific because it has receptor proteins that have active sites that are specific for binding to molecules
146
Exocytosis
Molecules are removed from the cell into the extracellular environment by using a vesicle, removing the molecule, and then becoming part of the membrane; exact opposite of endocytosis
147
Carbohydrates
Organic (meaning they are made of carbon) sugars that are used to make energy (ATP)
148
Monosaccharide
The monomers for carbohydrates; a single sugar
149
Types of monosaccharides
1. Glucose
2. Fructose
3. Galactose
150
Disaccharide
Two monosaccharides put together; two sugars
151
Two examples of disaccharides
1. Glucose + fructose = sucrose
| 2. Glucose + galactose = lactose
152
Polysaccharide
Many monosaccharides put together
153
Examples of polysaccharides
1. Glycogen: Many glucose monomers (molecules) put together that is used to store carbohydrates
2. Cellulose: A polysaccharide made by plants that humans cannot break down
154
Dehydration synthesis
Joins two molecules together (to make di- and poly- saccharides) by the removal of a water molecule
155
Hydrolysis
Breaks down the complex sugars by adding a water molecule
156
Types of lipids
1. Fatty acid
2. Triglyceride
3. Phospholipid
4. Steroid
157
Fatty acid
Hydrocarbon chain, long carbon chains that have hydrogen that soak up the electrons; has a carboxyl group attached
158
Fatty acid function
Energy, ATP
159
How do fatty acids help the body with ATP/energy
If glucose is low, our body can make ATP from lipids
160
What is the exception to lipids making energy
Neural system doesn't use lipids very well, needs glucose
161
How do fatty acids compare to glucose
Compared to glucose, fatty acids can store more energy because glucose is hydrophilic and needs to be stored with water, but lipids are hydrophobic and can be stored without water
162
How are carbon molecules in lipids linked together
Covalent bonds
163
Saturated
Lipid where every carbon linked with one covalent bond
164
Unsaturated
Lipid where there is a double covalent bond, has a kink in the structure
165
What type of lipid is able to be stored more efficiently and easily?
Saturated lipids; they are straight and easier to pack together
166
Triglyceride
3 fatty acids (tri) that are connected with a glycerol (glyceride)
167
How are the fatty acids attached to glycerol and broken down
Hydrolysis; adds a water molecule to bond the fatty acids with glycerol
Dehydration synthesis; takes away a water molecule to break down the triglyceride
168
What cells store triglycerides?
Adipocytes
169
Triglyceride function
Energy, used to store fatty acids (they are stored as triglycerides), insulation, protection
170
Phospholipid
2 fatty acids attached to a phosphate group; amphipathic
171
Phospholipid function
Used in the plasma membrane to create a phospholipid bilayer and protect the hydrophobic parts (heads are hydrophilic, tails are hydrophobic)
172
What do unsaturated lipids and saturated lipids do to the plasma membrane
To decrease fluidity, you make the membrane more saturated and to increase fluidity you make the membrane more unsaturated
173
Steroid function
Used for communcation
174
Why do steroid lipids all look the same
Because they are made from cholesterol
175
Cholesterol (lipids)
The building block of steroids and is modified to make different types
176
Types of steroids
1. Estrogen (puberty; menstrual cycle)
| 2. Testosterone (puberty; makes you either male or female)
177
Nucleic acids function
Used to store information
178
Types of nucleic acids
1. DNA
| 2. RNA
179
What kind of information does DNA and RNA store?
Information to make a protein
180
Nucleotide
The monomer of nucleic acid
181
Parts of a nucleotide
1. Sugar group (different for DNA and RNA)
2. Phosphate group
3. Nitrogenous base (Makes nucleotides different from one another)
182
Deoxyribose
The sugar in DNA
183
Ribose
The sugar in RNA
184
2 classes of nitrogenous bases
1. Purines (1 ring)
| 2. Pyrimines (2 rings)
185
Purine bases
1. Adenine
| 2. Guanine
186
Pyrimine bases
1. Cytosine
2. Thymine
3. Uracil
187
Nitrogenous bases in DNA
1. Adenine
2. Guanine
3. Cytosine
4. Thymine
188
Nitrogenous bases in RNA
1. Adenine
2. Guanine
3. Cytosine
4. Uracil
189
How are nucleotides linked together to form a polymer?
Phosphodiester bond
190
Phosphodiester bond
The phosphate bonds with the sugar group to form this covalent bond that links nucleotides together
191
What holds the two bases on each strand together?
Hydrogen bonds; weak
192
Why are the hydrogen bonds weak?
So that they can be pulled apart and replicated
193
DNA strands are
Complimentary
194
Why is it important that DNA is complimentary
In replication when the enzyme is reading one strand, it knows that the other side is exactly the same/opposite bases
195
What is the shape of DNA
Double helix
