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BIO 206: PHYSIOLOGY > Unit 1 > Flashcards

Unit 1 Flashcards

1
Q

What does NADH stand for and what does it do?

A

Nicotinamide adenine dinucleotide + hydrogen. It is a molecule

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2
Q

What is the rate limiting enzyme for the ATP-CP energy pathway?

A

Creatine kinase

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3
Q

What are the substrates required in glycolysis?

A

Glucose and 2 ATP

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4
Q

What are the products from glycolysis?

A

4 ATP (2 net ATP), 2 pyruvate, 2 NADH

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5
Q

What is the rate limiting enzyme for glycolysis?

A

Phosphofructokinase

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6
Q

What is the substrate of the citric acid cycle?

A

Acetyl CoA

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7
Q

What are the products of the citric acid cycle?

A

ATP, 3 NADH, 2 carbon dioxide, FADH2

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8
Q

What is the rate limiting enzyme of the citric acid cycle?

A

Isocitrate dehydrogenase

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9
Q

Where in the cell & under what conditions (aerobic or anaerobic) does the ATP-CP System operate?

A

In the cytosol – anaerobic

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10
Q

Where in the cell & under what conditions (aerobic or anaerobic) does Glycolysis operate?

A

In the cytosol – anaerobic

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11
Q

Where in the cell & under what conditions (aerobic or anaerobic) does the Citric Acid Cycle operate?

A

In the mitochondrial matrix – aerobic

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12
Q

Where in the cell & under what conditions (aerobic or anaerobic) does the Electron Transport System operate?

A

Within the mitochondria–aerobic

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13
Q

What is produced or released for the energy pathway ATP-CP System?

A

ATP & Creatine

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14
Q

What is produced or released for the energy pathway of Glycolysis?

A

4 ATP (Adenosine triphosphate); 2 net gain. 2 Pyruvate. 2 NADH. (Nicotinamide adenine dinucleotide + hydrogen)

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15
Q

What is produced or released for the energy pathway Citric Acid Cycle?

A

1 ATP, 1 FADH2 (flavin adenine dinucleotide), 2 CO2, 3 NADH.

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16
Q

What is produced or released for the energy pathway of the Electron Transport System?

A

26-28 ATP. 6 H2O.

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17
Q

What is the time to fatigue for the ATP-CP System?

A

10 - 15 seconds.

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18
Q

What is the time to fatigue for Glycolysis?

A

60 - 90 seconds.

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19
Q

What is the time to fatigue for the Citric Acid Cycle?

A

A few hours.

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20
Q

What is the time to fatigue for the Electron Transport System?

A

A few hours.

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21
Q

What is the rate-limiting enzyme for the Citric Acid Cycle?

A

Isocitrate dehydrogenase.

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22
Q

What is the rate-limiting enzyme for the Electron Transport System?

A

Cytochrome oxidase.

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23
Q

For aerobic pathways, where is the oxygen used/required for the Citric Acid Cycle?

A

Aerobic–to transport pyruvate into the mitochondrial matrix.

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24
Q

For aerobic pathways, where is the oxygen used/required for the Electron Transport System?

A

Binds with Hydrogen at the end of the Electron Transport system to form H2O.

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25
Q

What is a stimulus?

A

Any physiological change that deviates from the bodyʼs preferred set point. EXAMPLES: - Change in body temperature
- Change in body position or muscle tension
- Change in blood pressure
- Change in the concentration of certain
molecules or ions (glucose, O2, H+, Na+, etc.)

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26
Q

What is a sensor?

A

The structure that specifically detects
the change from a set point (stimulus). EXAMPLES: Protein receptors on cell membranes
- Sensory receptors or specialized cells
distributed strategically throughout the
body
> Chemoreceptors
> Thermoreceptors
> Osmoreceptors
> Proprioceptors
> Baroreceptors
> Photoreceptors

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27
Q

What is the integrating center?

A
  • The anatomical location/structure where information from the sensor is interpreted or compared to a stored set-point
    > When the integration center analyzes sensory data, it determines the optimal solution to the problem
    EXAMPLES:
    > Individual proteins
    > Specific regions of the central nervous system
    > Specific endocrine glands or cells
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28
Q

What is an effector?

A
  • The specific anatomical structure that can counteract the stimulus and return the affected body parameter to its set point
  • Cued into action by the integrating center via a specific neural or endocrine efferent pathway
    EXAMPLES:
    > enzymes
    > organelles
    > skeletal muscle, distal nephron
    > organs, like sweat glands
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29
Q

What are the substrates of the electron transport system?

A

Hydrogen ions, high-energy electrons (from NADH and FADH2)

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30
Q

What is the effector’s action?

A

The effector is an anatomical structure
EXAMPLES:
> sweat gland secreting sweat
> specific muscle contracting

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31
Q

What is a response?

A

The outcome of the effectorʼs action. The goal is being worked toward. The OPPOSITE of a stimulus in a negative feedback loop. For a positive, requires an outside factor to intervene and shut it off.

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32
Q

What are the components of an atom? Which are located in the nucleus? Where do the e- exist?

A

Protons (+), electrons (-), and neutrons (no charge). N+P = in the nucleus. E- exist in orbitals or shells.

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33
Q

What are the major essential elements for life?

A

C, H, O, N, P, Ca, Na, K, Cl, S, Mg

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34
Q

What are the minor or trace essential elements?

A

Selenium, molybdenum, manganese, chromium, iodine

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35
Q

–> atomic number 7
–> chemical sym. N
–> atomic weight 13
What does the atomic number tell you?

A

OF PROTONS IN AN ATOM. And therefore what atom it is.

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36
Q

–> atomic number 7
–> chemical sym. N
–> atomic weight 13
What does the atomic mass or weight tell you?

A

The sum of N+P in an atom. Units of measurement = 1 atomic mass unit (amu)

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37
Q

What are isotopes?

A

Variations of an element that differ in mass. Same # of protons, but neutrons vary

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38
Q

What are ions?

A

Charged atoms

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39
Q

What are cations?

A

Positively charged ions (+)… LOST electrons

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40
Q

What are anions?

A

Negative charged (-)…GAINED electrons

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41
Q

Name 4 things electrons can do?

A
  1. Lead to the formation of ions.
  2. Allow for the formation of COVALENT bonds.
  3. Can become high-energy electrons, like when making ATP.
  4. Can lead to the formation of free radicals, which are unstable atoms or molecules with one or more unpaired electrons.
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42
Q

Describe 4 types of chemical bonds?

A
  1. Covalent (strong)
  2. Ionic
  3. Hydrogen (weak)
  4. Van der Waals forces (very weak)
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43
Q

What is the name of the bond between two monosaccharides?

A

A glycosidic bond

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44
Q

What makes a covalent bond “nonpolar?”

A

Electrons shared equally between atoms

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45
Q

What is the name of the bond that connects glycerol to fatty acids?

A

Ester bonds

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46
Q

What makes a covalent bond “polar”?

A

One atom in the molecule has

stronger pull on the shared electrons

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47
Q

What is an ionic bond?

A

Transfer of an electron(s) from one atom to

another, like in NaCl

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48
Q

What are some common cations in physiology?

A

Na+, K+, Ca2+, H+, Mg2+

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49
Q

What are some common anions in physiology?

A

Cl-, HCO3- (bicarbonate), HPO4,2- (phosphate) & SO4,2- (sulfate)

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50
Q

This kind of bond readily breaks in an aqueous environment.

A

Hydrogen bond

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51
Q

This bond is the strongest in an aqueous

environment, often needing enzymes or high temperatures to be broken.

A

Covalent bonds

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52
Q

This weak bond can form between any two

atoms, as long as their nuclei are close enough.

A

Van der Waals forces

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53
Q

This bond typically exists between polar

covalent molecules, like water.

A

Ionic bonds

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54
Q

What is the normal pH range for human blood? Is it neutral, acidic, or basic?

A

7.35 to 7.45, with the average at 7.40.

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55
Q

What is the role of buffers? What is the primary buffer in human blood?

A

Buffers minimize changes of pH. Bicarbonate ion (HCO3-).

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56
Q

What is a biomolecule? Also, name all 4.

A 
Biomolecules are a subset of 
organic molecules that are 
important in living organisms.  
1. Carbohydrates.
2. Lipids.
3. Nucleotides/nucleic acids
4. Proteins
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57
Q

What is the simplest form or unit of a biomolecule? What is it’s nickname as well?

A

A MONOMER!!! “Building-blocks”

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58
Q

Define a polymer.

A

Chain of two or more biomolecule monomers

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59
Q

What is the most abundant biomolecule?

A

Carbohydrates

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60
Q

What is the monomer (also called simple sugars) of carbohydrates?

A 
Monosaccharides.
EXAMPLES: 
> Glucose
> Fructose
> Ribose
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61
Q

What is the polymer (also called “complex carbohydrates”) of Carbohydrates?

A

Polysaccharides.
EXAMPLES:
> Glycogen – storage form of carbohydrates in animals
> Starch – storage form of carbohydrates in plants
> Cellulose – dietary fiber, non-digestible by humans

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62
Q

What is the name of the bond that links individual nucleotide monomers to nucleic acid polymers?

A

phosphodiester bonds

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63
Q

What is the intermediate level of Carbohydrates?

A

> Disaccharides: Made up of 2 monosaccharides

> Oligosaccharides: Made up of a few (e.g., 3 - 10) monosaccharides

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64
Q

What is the name of the bond between two monosaccharides?

A

A glycosidic bond

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65
Q

What is the monomer of Lipids?

A

Fatty acids.

> Can be saturated or unsaturated

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66
Q

What is the polymer of lipids?

A

Monoglycerides, diglycerides, and triglycerides.

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67
Q

What are nucleotides and their function?

A

Nucleotides are composed of a nitrogenous base, a monosaccharide, and a phosphate functional group. Their function is to use genetic recipes for building cellular proteins. Can be used as signal molecules.

68
Q

What are the 5 nitrogenous bases in nucleotides?

A

A denine
T hymine (in DNA only, instead of Uracil)
G uanine
C ytosine
U racil (in RNA only, instead of Thymine)

69
Q

What is the name of the bond between individual amino acids?

A

A peptide bond

70
Q

Which monosaccharides are used in nucleotides?

A

Deoxyribose (in DNA)

Ribose (in RNA)

71
Q

What is the polymer of nucleotides/nucleic acids?

A

DNA & RNA

72
Q

What is the monomer for Proteins? (The workers of your cells, and most versatile biomolecule)

A

Amino acids (AAs) = building blocks of all proteins. 9 essential, 11 non essential.

73
Q

What are the 5 polymers for proteins called?

A
  1. Dipeptides (2 amino acids)
  2. Tripeptides (3 amino acids)
  3. Oligopeptides (4 – 9 amino acids)
  4. Polypeptides (10 – 100 amino acids)
  5. Proteins (>100 amino acids)
74
Q

Describe the PRIMARY level of protein organization.

A

The primary structure is the specific sequence of amino acids in a peptide
> This linear sequence of amino acids determines what all higher levels of structure (secondary, tertiary and quaternary) will look like

75
Q

Describe the secondary level structures that emerge when nearby amino acids chemically interact.

A

Alpha helix or beta pleated sheet.
> Formed if a particular primary structure/sequence of amino acids exists
> Bonds at one point in the chain attract or repel other amino acids elsewhere in the chain (see previous slide)
> Alpha helices are the typical secondary structure in globular proteins that perform cellular work

76
Q

Describe the tertiary level of protein organization.

A

Bending and folding of the secondary level structures relative to each other to form the most stable structure in an aqueous environment. Allows the protein to form a complex, three-dimensional structure. Can create globular proteins

77
Q

Describe the quaternary level of protein organization.

A 
Formed when 2 or more tertiary-
level structures (subunits) are 
attached to form a fully-functional 
molecule
> Hemoglobin is a 
great example of 
the quaternary 
level of protein 
structure
78
Q

Name some common factors that affect protein structure.

A
  1. Temperature: affects bond strengths
  2. pH: Hydrogen ions (H+) in solution, because of their positive charge, can alter molecular structure
  3. Drugz: Can covalently attach to proteins and change their
    structure
79
Q

What are the three main body cavities (structural/ anatomical compartments)?

A

Cranial, thoracic, and abdominopelvic cavities

80
Q

Fatty acids are the monomer form of

what biomolecule category?

A

Lipids

81
Q

This category of biomolecule carries out
diverse jobs within the cell, such as
energy storage, communication, and
information storage.

A

Nucleotides/nucleic acids.

82
Q

Polymers in this biomolecule category

have four levels of structural complexity.

A

Proteins

83
Q

Sucrose and glucose are examples of this

biomolecule category.

A

Carbohydrates

84
Q

Steroid hormones are part of this

biomolecule category.

A

Lipids

85
Q

What are the 7 functional categories of proteins?

A 
E nzymes
M embrane transporters
S ignal molecules
R eceptors
B inding proteins
I mmunoglobulins
R egulatory proteins
86
Q

What is the lumen?

A

The interior space of hollow organs

87
Q

What do enzymes do?

A

Catalyze (speed up) chemical reactions

88
Q

What do membrane transporters two? What are the two types?

A

Move polar substances across cell membranes. Two types: channels or carrier proteins

89
Q

what is the intracellular fluid?

A

fluid inside of the cell

90
Q

What is an example of signal molecules?

A

Hormones or neuropeptides

91
Q

What is the role of receptors?

A

Bind signaling molecules. Trigger a change in cell function

92
Q

What do binding proteins do? Name two examples.

A

Bind and transport nonpolar molecules around the body’s aqueous environment
Examples: hemoglobin, lipoproteins, etc.

93
Q

What type of compartments are physiologists focused on?

A

Functional compartments

94
Q

What is the alternate name for immunoglobulins? What are their role?

A

Also called antibodies. Involved in the immune response

95
Q

What is the extracellular fluid?

A

Fluid outside of the cell

96
Q

Role of regulatory proteins and what is their alternate name?

A

Regulate of gene expression and protein synthesis. Also called transcription factors

97
Q

The molecule or ion that it binds is generally called a _________. Or a _______ if it binds to an enzyme or membrane transporter.

A

Ligand; substrate

98
Q

Name and describe the several important principles of protein-ligand interactions.

A

Affinity
> Reflects the strength of the attraction and bond between molecules
> Strongly attached (high affinity) vs. likely to dissociate (low affinity)
Specificity
> The protein and ligand must be structurally compatible
> Proteins bind to specific ligands or a group of related ligands like a “lock and key”
Ÿ» Some proteins are more specific (or limited) in what they can bind than others

99
Q

What is protein modulation?

A

“Modulation” means to either increase or decrease the activity of a protein

100
Q

What are the two types of extracellular fluid and where are they located?

A

Plasma - fluid in blood vessels

Interstital fluid - surrounds most body tissue cells

101
Q

What are some ways to modulate the action of cellular proteins?

A

Increase or decrease protein action

102
Q

What are the protein modulators that INCREASE (activators) the action called? List all of their subtypes.

A
  1. Proteolytic (lyse = break or rupture)
  2. allosteric
  3. cofactors
  4. covalent
103
Q

What are the four functions of the cell membrane?

A

A selectively permeable barrier; gateway for exchange between intra and extracellular compartments; communication from cell to cell; cell and tissue structure.

104
Q

What are the protein modulators that DECREASE (inhibitors) the action called? List all of their subtypes.

A
  1. Proteolytic
  2. allosteric
  3. competitive
  4. covalent
105
Q

What is covalent modulation?

A

Attachment of atoms or
functional groups to
modulate proteins

106
Q

How would a protein cell avoid the problem of saturation?

A

If a cell adds more protein workers, then
it can get more work done and avoid the
problem of saturation. Increasing the [protein] is called up-
regulation.
> Upregulation is accomplished through
the process of protein synthesis

107
Q

This category of proteins can activate and

inactivate genes, which will change the levels of protein workers in cells.

A

Regulatory proteins

108
Q

What is the cell membrane composed of?

A

A phospholipid bilayer, cholesterol, and embedded proteins

109
Q

These protein categories are involved in cell-to-cell communication. List them all.

A

Receptors, signal molecules, binding proteins.

110
Q

Proteins in this category catalyze chemical

reactions.

A

Enzymes

111
Q

Molecules, especially nonpolar ones, are moved around the body by these types of proteins.

A

Binding Proteins.

112
Q

What are the two general types of proteins contained in the cell membrane?

A

Integral proteins and peripheral proteins

113
Q

Why do humans and other organisms need energy?

A

Energy is needed to do work

114
Q

What kind of work does the body perform? List all 3.

A

Chemical work
> Making and breaking of chemical bonds
Transport work
> Moving substances into or out of cells and around the body
> Creation of concentration gradients (especially for ions)
»Necessary for cell activation (like for neural, endocrine, or muscle
cells)
Mechanical work
> Movement, such as muscle contractions that allow the body to
move or movement of organelles from point A to point B within the
cell

115
Q

WHO does the work of the cells?

A

Proteins, and they need a lot of ENERGY to do the work

116
Q

What are the two types of integral proteins in the cell membrane, where are they located, and how are they removed from the membrane?

A

transmembrane proteins - span the membrane from one side to the other
lipid anchored proteins - present only on one side, but are congugated to lipid tails embedded in the membrane
Can only be removed by disrupting the membrane with detergents or other harsh methods

117
Q

What are the two states of energy? Describe them.

A
  1. Kinetic - energy in motion or action

2. Potential energy (free energy) - STORED energy

118
Q

What is entropy?

A

All processes naturally move from state of order to disorder

119
Q

ATP –> ADP + Pi + Energy is an example of….

A

An EXergonic chemical reaction, where free energy is released from
broken chemicals bond in the
reactant(s)

120
Q

ADP + Pi + Energy –> ATP is an example of what chemical reaction?

A

ENDERgonic, where some of the activation energy is retained and added to the product’s free energy by creating new
chemical bonds

121
Q

The energy to create new bonds often comes from one or more is called _______.

A

COUPLED REACTIONS

122
Q

Where are peripheral proteins located and are they easily seperated from the cell membrane?

A

only on one side of the membrane, attached to an integral protein or a phosphate head by noncovalent bonds
can be seperated from the membrane without damaging the membrane

123
Q

What is metabolism?

A

The sum of all energy exchanges in an organism

124
Q

What are the two phases of metabolism?

A

Catabolism - breakdown of large, complex biomolecules into simpler forms
Anabolism - Synthesis of larger molecules from smaller ones to store free energy in new chemical bonds

125
Q

What components of the cell membrane are considered “congugated”?

A

phospholipids

126
Q

True or False: ATP is stored within the body.

A

FALSE. It only lasts - 5 seconds and must be replaced as quickly as itʼs used

127
Q

ATP –> ADP + Pi + Energy is called…

A

This is called ATP hydrolysis. Energy then used for cellular work, some lost
as heat

128
Q

What are the two anaerobic energy pathways?

A

ATP-CP System

Glycolysis

129
Q

Which molecules of the cell membrane have a polar and a nonpolar end?

A

phospholipids and cholesterol

130
Q

True or false: anaerobic = doesn’t require O2

A

TRUE

131
Q

True or false: aerobic = requires O2

A

TRUE

132
Q

What are the two aerobic energy pathways?

A

Citric Acid Cycle (Krebs Cycle)

Electron Transport System

133
Q

What proteins in the cell membrane are in direct contact with the intra- and extracellular compartments?

A

transmembrane proteins

134
Q

True or False: All energy pathways are functioning all of the time.

A

True. One or two might be primary (or more active) depending
on the conditions, but the others still contribute to some
degree

135
Q

Where do aerobic pathways take place?

A

In the mitochondria

136
Q

Which end (polar or nonpolar) of a phospholipid faces the inside or the outside of the cell

A

The polar end

137
Q

Where do anaerobic pathways take place?

A

In the cytosol.

138
Q

Oxygen combines with H+ at the end of this pathway.

A

Electron Transport System.

139
Q

Carbon dioxide is produced by this pathway.

A

Citric Acid Cycle

140
Q

These pathways do not require oxygen.

A

ATP-CP System, Glycolysis

141
Q

These pathways DO require oxygen.

A

Citric Acid/Krebs Cycle, Electron Transport System

142
Q

NADH and FADH2 are oxidized in this pathway.

A

Electron Transport System

143
Q

What are inclusions? Give some examples and a brief definition

A

Inclusions are insoluble particles in the cell that don’t have any sort of membrane.
Ribosomes - location where amino acids are assembles into peptides/ proteins
Proteasomes - Enzymes that break down proteins that are no longer needed
Intracellular fuels - i.e. glycogen, lipid droplets
Protein fibers - filaments and tubules - cilia, cytoskeleton, contractile proteins

144
Q

What makes up the cytoskeleton?

A

Protein fiber inclusions. Such as microfilaments, intermediate fibers, and microtubules.

145
Q

What is the function of the cytoskeleton?

A

Determines cell shape, internal organization, assembly of cells and tissues, cell membrane movement, and intracellular transport.

146
Q

What is the function of motor proteins?

A

Move organelles and other structures around the cell by walking down the cytoskeleton as a road. Use energy from ATP to create movement. 

147
Q

Why do membrane-bound organelles have membranes?

A

To enable protected chemical reactions.

148
Q

What is the job of the mitochondria? What processes does it use.

A

Generates ATP for cell energy through aerobic processes. The powerhouse of the cell.

149
Q

Difference between Rough ER and Smooth ER:

A

Rough ER: Ribosomes on external surface give the “rough”appearance
Smooth ER: Lipid and fatty acid synthesis

150
Q

This cell structure is responsible for the synthesis of lipids:

A

SMOOTH ER

151
Q

This cell structure is responsible for the synthesis of proteins:

A

Ribosomes

152
Q

This cell structure is responsible for the packaging of proteins for transport

A

Golgi complex

153
Q

This cell structure is responsible for the housing of genetic material of the cell

A

Nucleus

154
Q

This cell structure is responsible for the site of aerobic respiration

A

Mitochondria

155
Q

This cell structure is responsible for the post-translational modification of proteins

A

ROUGH ER

156
Q

This cell structure is responsible for giving the cell structure and enables membrane movement

A

Cytoskeleton

157
Q

This cell structure is filled with molecules for secretion or storage

A

Cytoplasmic vesicles

158
Q

What are gap junctions?

A

Channels that connect cytoplasm of two adjacent cells

> Permit chemical & electrical signals to pass from one cell to the next VERY QUICKLY

159
Q

What are tight junctions?

A

As the name suggests, the restrict movement between adjacent cells
> Create barriers that help regulate movement of substances

160
Q

What are desmosomes?

A

Button-like, anchoring junctions – help cells form strong tissues

161
Q

What are the three things that make up nucleotides?

A

Nitrogenous bases, a 5-carbon sugar, and one or more phosphate groups

162
Q

Which nitrogenous bases are purines?

A

Adenine and Guanine

163
Q

Which nitrogenous bases have pyrimidine structures?

A

Cytosine
Thymine
Uracil

164
Q

What forms the backbone of DNA and RNA?

A

Sugar-phosphate

165
Q

Name 3 disaccharides and their monomers.

A

Sucrose - glucose + fructose
Maltose - glucose + glucose
Lactose - glucose + galactose

166
Q

What are the two types of membrane transporter proteins?

A

channels

carrier proteins

BIO 206: PHYSIOLOGY (9 decks)

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