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A&P > Lecture Exam 1 > Flashcards

Lecture Exam 1 Flashcards

1
Q

Anatomy

A

Structure, how things look

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2
Q

Levels of Anatomy

A
  1. Gross Anatomy

2. Microscopic Anatomy

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3
Q

Gross Anatomy

A

The level of anatomy that you can see with your eyes

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4
Q

Example of Gross Anatomy

A

Cadaver labs

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5
Q

Microscopic Anatomy

A

Below the level of what you can see with your eyes

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6
Q

Examples of Microscopic Anatomy

A
  1. Cytology: Study of cells

2. Histology: Study of tissues

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7
Q

What is cytology used for

A

Pathologists use cytology to tell if something looks normal or abnormal

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8
Q

Physiology

A

Function, what it does

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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
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10
Q

Hierarchy of Life

A
  1. Molecular/Chemical Level
  2. Cellular Level
  3. Tissue Level
  4. Organ Level
  5. Organ System
  6. Organism
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11
Q

Example of Molecular/Chemical Level

A

Atoms

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12
Q

Cellular level

A

Molecules that are formed together

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13
Q

Example of tissue level

A

Histology

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14
Q

Tissue Types

A
  1. Epithelial (Found in skin)
  2. Muscle
  3. Connective
  4. Neural
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15
Q

Organ level

A

Multiple tissues that come together

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16
Q

Example of organ level

A

Heart

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17
Q

How many organ systems do we have

A

11

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18
Q

Example of organ system

A

Digestive system

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19
Q

Example of organism

A

Humans

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20
Q

What is the function of the organism

A

To maintain homeostasis

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21
Q

Homeostasis

A

Having a stable internal environtment

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22
Q

Things to keep in homeostasis

A
  1. Body temperature
  2. pH of body and blood
  3. Blood pressure
  4. Heart rate
  5. Respiratory rate
  6. Water
  7. Blood sugar
  8. Sodium
  9. Potassium
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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

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24
Q

Static equilibrium

A

If your body temperature stayed the same

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25
Q

Dynamic equilibrium

A

Not the same everyday (changes). There is a range that is accepted

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26
Q

Why do you shiver?

A

Muscle contractions heat you up

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27
Q

Ways to Maintain Homeostasis

A
  1. Autoregulation

2. Extrinsic regulation

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28
Q

Autoregulation

A

Regulation without help

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29
Q

Examples of autoregulation

A

Stomach
- Food puts off homeostasis, so it undergoes homeostasis to digest it
Running
- Blood to the heart increases by itself

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30
Q

Extrinsic regulation

A

Regulation with help

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31
Q

Where does the help for extrinsic regulation usually come from

A

Neural and endocrine systems

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32
Q

Types of Extrinsic Regulation

A
  1. Feed-forward

2. Feed-back

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33
Q

Feed-forward

A

The ability to predict a change in homeostasis and begin to prepare for it before it happens

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34
Q

Examples of feed-forward

A

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

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35
Q

Types of Feedback (Loops)

A
  1. Positive feedback loop

2. Negative feedback loop

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36
Q

Positive feedback loop

A

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

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37
Q

Examples of positive feedback loops

A

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

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38
Q

Negative feedback loop

A

Body’s response to a stimulus is to revert the stimulus; The most important/most common type of regulation

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39
Q

What is the body’s first response to a stimulus

A

Recognizing the stimulus

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40
Q

Receptors

A

Recognizes a stimulus and sends information to the integration center

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41
Q

Integration center

A

(The brain, usually) Takes in information and determines if a response is necessary; If a response is necessary it sends information to the effector

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42
Q

Effector

A

Acts on the stimulus (exaggerates or counteracts)

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43
Q

Types of macromolecules

A
  1. Proteins
  2. Lipids
  3. Carbohydrates
  4. Nucleic acids
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44
Q

Macromolecules

A

Organic; which means that it has carbon

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45
Q

What looks just like carbon

A

Silicon

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46
Q

What is unique about carbon?

A

The carbon bonds can twist and go from something long and linear and make them into rings

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47
Q

Macromolecules are

A

Polymers

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48
Q

Polymers

A

Big structures that are made from smaller individual units

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49
Q

Monomer

A

Individual units that make a polymer

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50
Q

What is the monomer that is used to make proteins?

A

Amino acids

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51
Q

How many amino acids are in our body?

A

At least 20

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52
Q

What makes amino acids different from each other?

A

Different R group

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53
Q

Pieces of an Amino Acids:

A
  1. Amino group
  2. Central carbon
  3. Carboxyl group
  4. R group (variable side chain of one or more atoms)
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54
Q

What is dependent on the R group

A

The chemical properties of an amino acid

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55
Q

How do you link 2 amino acids?

A

By freeing up a bond on both amino acids and then linking the carboxyl group to the amino group

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56
Q

Every atom has a limited

A

Amount of bonds it can make

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57
Q

Peptide bond

A

A strong covalent/chemical bond that links amino acids by linking a carboxyl and amino group

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58
Q

What does the digestive system do with peptide bonds?

A

It breaks it down so that we can absorb it

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59
Q

Dehydration synthesis

A

When the amino acid loses a molecule of water to make a peptide bond

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60
Q

Hydrolysis

A

The opposite of dehydration synthesis; When you add a molecule of water to break down a peptide bond

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61
Q

Protein Structures:

A
  1. Primary structure
  2. Secondary structure
  3. Tertiary structure
  4. Quaternary structure
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62
Q

Primary structure

A

Chain of amino acids that are all linked together by peptide bonds that is not functional

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63
Q

What must happen for a protein to be functional

A

It must turn into a 3D structure

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64
Q

Secondary structure can either be in the form of:

A
  1. Alpha-helix

2. Beta-sheets

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65
Q

What is the driving force of the secondary structures?

A

The formation of hydrogen bonds; which are weak bonds

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66
Q

Secondary structures can be a

A

Combination of alpha-helix and beta-sheet structures

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67
Q

Hydrophobic interactions

A

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

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68
Q

Quaternary structure

A

Two or more tertiary structures that have come together

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69
Q

A protein is only functional if

A

It folds into the correct shape

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70
Q

Example of mutation of protein strucuture

A

Sickle cell anemia: An inherited mutation of hemoglobin where one amino acid is changed. This messes with the hydrogen bonds and the structure/shape

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71
Q

Catalyst

A

Anything that speeds up a chemical reaction but is not used up in the reaction

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72
Q

Activation energy

A

Energy that is needed to get a chemical reaction moving

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73
Q

Example of activation energy

A

Stirring sugar in water

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74
Q

Enzymes

A

Protein catalysts that our body uses that can be reused over and over

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75
Q

What is the function of enzymes

A

To make chemical reactions happen fast enough to maintain life

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76
Q

Process of an enzyme:

A
  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
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77
Q

Active site

A

Pockets that are formed from the what that the protein forms

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78
Q

What do enzymes do

A

Lower the amount of activation energy required

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79
Q

Factors that influence enzyme activity

A
  1. pH

2. Temperature

80
Q

Every enzyme has an…

A

Optimal temperature

81
Q

When do enzymes not work as well

A
  1. Colder temperature

2. Hotter temperature

82
Q

What happens to enzymes in colder temperatures

A

They slow down

83
Q

What happens to enzymes in hotter temperature

A

It denatures

84
Q

Denature

A

The 3D structure breaks down and it reverts to its primary structure

85
Q

What happens when an enzyme denatures

A

The hydrophobic amino acids go into the water and are unprotected

86
Q

Example of denature of a protein/enzyme

A

Eggs: When they are cooked, the protein in them breaks down and it turns from clear to white

87
Q

Salivary amylase

A

An enzyme that degrades carbohydrates; found in saliva; works best as around pH 7, when food is swallowed it doesn’t work well

88
Q

Pepsin

A

An enzyme in the function that has an optimal pH of about 2; shows that enzymes need a specific environment

89
Q

2 ways a drug can block an enzyme

A
  1. Competitive inhibition

2. Non-competitive inhibitions

90
Q

Competitive inhibition

A

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
Q

Non-competitive inhibitions

A

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
Q

What does homeostasis do for enzymes

A

It creates the perfect environment for the enzymes

93
Q

What is the inside of the plasma membrane

A

Cytoplasm

94
Q

What is the outside of the plasma membrane called

A

Extracellular part

95
Q

What separates the outside and inside region

A

The plasma membrane

96
Q

Importance of the plasma membrane

A
  1. Gives physical isolation

2. Provides a chemical boundary

97
Q

How does the membrane help with the internal conditions of the cell

A

It establishes conditions within the cell that are optimal for metabolism

98
Q

What is the main function of the plasma membrane

A

It is the ultimate gatekeeper, it determines what gets in and out of the cell

99
Q

What are the major structures of the plasma membrane

A
  1. Phospholipids
  2. Proteins
  3. Cholesterol
100
Q

Major parts of phospholipids

A
  1. Lipid tails/fatty acid chain/hydrocarbon chain
  2. Glycerol (tails are attached to this)
  3. Phosphate group
101
Q

Hydrocarbon chain

A

Means it is made of carbon linked together and hydrogens that soak up the electron

102
Q

Most lipids are

A

Hydrophobic

103
Q

Phospholipids are

A

Amphipathic

104
Q

Amphipathic

A

Parts of the molecule are hydrophobic and parts are hydrophilic

105
Q

Three ways phospholipids organize

A
  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
Q

Bilayer

A

The plasma membrane is a phospholipid bilayer

107
Q

What molecules pass through the plasma membrane freely

A

Hydrophobic

108
Q

Two classes of proteins

A
  1. Integral protein: Spans the entire plasma membrane bilayer
  2. Peripheral protein: On the inside, does not span the lipid bilayer
109
Q

What is the importance of proteins in the plasma membrane?

A

They facilitate membrane transport, the hydrophilic molecules move through these protein channels

110
Q

The plasma membrane is

A

Fluid, or always moving

111
Q

Fluid-mosaic model

A

Describes the moving plasma membrane

112
Q

What is the purpose of cholesterol?

A

To control the fluidity or movement of the plasma membrane

113
Q

How things move in and out of the cell

A
  1. Simple diffusion

2. Facilitated diffusion

114
Q

What do you need for simple diffusion to occur?

A

A concentration gradient

115
Q

Concentration gradient

A

Different amounts of concentration

- Things always move down the gradient, from high to low

116
Q

Brownian motion

A

Things are always moving, making things collide and bounce off of each other, causing diffusion

117
Q

What molecules move through the plasma membrane through simple diffusion

A

Small, hydrophobic molecules

118
Q

What molecules use facilitated diffusion

A

Large, charged molecules because they are hydrophilic

119
Q

Aquaporins

A

Pores that move water through facilitators back and forth across the plasma membrane

120
Q

Osmosis

A

Movement of water across a selectively permeable membrane

121
Q

Osmotic pressure

A

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
Q

Example of osmotic pressure

A
  • 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
Q

Tonicity

A

Describes the effect that a solution has on a cell

124
Q

Isotonic

A

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
Q

Hypotonic

A

Less solute in the solution than inside the cell, or more solute inside the cell than the outside (it is plump)

126
Q

Example of something hypotonic

A

Water

127
Q

Hypertonic

A

More solute outside the cell than inside

128
Q

Active transport

A

Moves things against the concentration gradient, from low to high; requires energy because it is not “natural”

129
Q

Sodium-potassium exchange pump

A

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
Q

Secondary Active Transport

A

The concentration gradient of one substance provides the driving force needed to give the second substance a free ride

131
Q

Glucose-sodium transporter

A

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
Q

What will happen to sodium over time if it only uses the glucose-sodium transporter?

A

It will reach equilibrium and stop moving down its gradient and stop glucose coming into the cell

133
Q

How does sodium not reach equilibrium?

A

It uses both the sodium-potassium pump and the glucose-sodium transporter

134
Q

Why is it called the secondary active transport?

A

Because it happens after the sodium-potassium pump and is dependent on it

135
Q

How many transporters do we have?

A

A limited amount, making there be a limit to the rate of transport that can occur

136
Q

As the concentration gradient gets larger (ex. More sodium on one side)

A

The rate of transport gets faster

137
Q

Why does the rate of transport stop getting faster?

A

Because we have a limited number of transporters and they are all being used

138
Q

What happens to blood that goes into the kidney tubules

A

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
Q

Vesicular transport

A

Materials are moved in or out of the cell using vesicles

140
Q

Types of vesicular transport

A
  1. Endocytosis

2. Exocytosis

141
Q

Endocytosis

A

Membrane makes a “bud” and pulls something in after it pinches off into the cell

142
Q

Types of endocytosis

A
  1. Pinocytosis
  2. Phagocytosis
  3. Receptor mediated
143
Q

Pinocytosis

A

Constantly randomly testing fluid from the environment that can be useful or useless

144
Q

Phagocytosis

A

Pulls in specific things by reaching out and capturing things from the environment

145
Q

Receptor mediated

A

Extremely specific because it has receptor proteins that have active sites that are specific for binding to molecules

146
Q

Exocytosis

A

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
Q

Carbohydrates

A

Organic (meaning they are made of carbon) sugars that are used to make energy (ATP)

148
Q

Monosaccharide

A

The monomers for carbohydrates; a single sugar

149
Q

Types of monosaccharides

A
  1. Glucose
  2. Fructose
  3. Galactose
150
Q

Disaccharide

A

Two monosaccharides put together; two sugars

151
Q

Two examples of disaccharides

A
  1. Glucose + fructose = sucrose

2. Glucose + galactose = lactose

152
Q

Polysaccharide

A

Many monosaccharides put together

153
Q

Examples of polysaccharides

A
  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
Q

Dehydration synthesis

A

Joins two molecules together (to make di- and poly- saccharides) by the removal of a water molecule

155
Q

Hydrolysis

A

Breaks down the complex sugars by adding a water molecule

156
Q

Types of lipids

A
  1. Fatty acid
  2. Triglyceride
  3. Phospholipid
  4. Steroid
157
Q

Fatty acid

A

Hydrocarbon chain, long carbon chains that have hydrogen that soak up the electrons; has a carboxyl group attached

158
Q

Fatty acid function

A

Energy, ATP

159
Q

How do fatty acids help the body with ATP/energy

A

If glucose is low, our body can make ATP from lipids

160
Q

What is the exception to lipids making energy

A

Neural system doesn’t use lipids very well, needs glucose

161
Q

How do fatty acids compare to glucose

A

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
Q

How are carbon molecules in lipids linked together

A

Covalent bonds

163
Q

Saturated

A

Lipid where every carbon linked with one covalent bond

164
Q

Unsaturated

A

Lipid where there is a double covalent bond, has a kink in the structure

165
Q

What type of lipid is able to be stored more efficiently and easily?

A

Saturated lipids; they are straight and easier to pack together

166
Q

Triglyceride

A

3 fatty acids (tri) that are connected with a glycerol (glyceride)

167
Q

How are the fatty acids attached to glycerol and broken down

A

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
Q

What cells store triglycerides?

A

Adipocytes

169
Q

Triglyceride function

A

Energy, used to store fatty acids (they are stored as triglycerides), insulation, protection

170
Q

Phospholipid

A

2 fatty acids attached to a phosphate group; amphipathic

171
Q

Phospholipid function

A

Used in the plasma membrane to create a phospholipid bilayer and protect the hydrophobic parts (heads are hydrophilic, tails are hydrophobic)

172
Q

What do unsaturated lipids and saturated lipids do to the plasma membrane

A

To decrease fluidity, you make the membrane more saturated and to increase fluidity you make the membrane more unsaturated

173
Q

Steroid function

A

Used for communcation

174
Q

Why do steroid lipids all look the same

A

Because they are made from cholesterol

175
Q

Cholesterol (lipids)

A

The building block of steroids and is modified to make different types

176
Q

Types of steroids

A
  1. Estrogen (puberty; menstrual cycle)

2. Testosterone (puberty; makes you either male or female)

177
Q

Nucleic acids function

A

Used to store information

178
Q

Types of nucleic acids

A
  1. DNA

2. RNA

179
Q

What kind of information does DNA and RNA store?

A

Information to make a protein

180
Q

Nucleotide

A

The monomer of nucleic acid

181
Q

Parts of a nucleotide

A
  1. Sugar group (different for DNA and RNA)
  2. Phosphate group
  3. Nitrogenous base (Makes nucleotides different from one another)
182
Q

Deoxyribose

A

The sugar in DNA

183
Q

Ribose

A

The sugar in RNA

184
Q

2 classes of nitrogenous bases

A
  1. Purines (1 ring)

2. Pyrimines (2 rings)

185
Q

Purine bases

A
  1. Adenine

2. Guanine

186
Q

Pyrimine bases

A
  1. Cytosine
  2. Thymine
  3. Uracil
187
Q

Nitrogenous bases in DNA

A
  1. Adenine
  2. Guanine
  3. Cytosine
  4. Thymine
188
Q

Nitrogenous bases in RNA

A
  1. Adenine
  2. Guanine
  3. Cytosine
  4. Uracil
189
Q

How are nucleotides linked together to form a polymer?

A

Phosphodiester bond

190
Q

Phosphodiester bond

A

The phosphate bonds with the sugar group to form this covalent bond that links nucleotides together

191
Q

What holds the two bases on each strand together?

A

Hydrogen bonds; weak

192
Q

Why are the hydrogen bonds weak?

A

So that they can be pulled apart and replicated

193
Q

DNA strands are

A

Complimentary

194
Q

Why is it important that DNA is complimentary

A

In replication when the enzyme is reading one strand, it knows that the other side is exactly the same/opposite bases

195
Q

What is the shape of DNA

A

Double helix

A&P (13 decks)

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