Unit 1 Flashcards
(166 cards)
1
Q
What does NADH stand for and what does it do?
A
Nicotinamide adenine dinucleotide + hydrogen. It is a molecule
2
Q
What is the rate limiting enzyme for the ATP-CP energy pathway?
A
Creatine kinase
3
Q
What are the substrates required in glycolysis?
A
Glucose and 2 ATP
4
Q
What are the products from glycolysis?
A
4 ATP (2 net ATP), 2 pyruvate, 2 NADH
5
Q
What is the rate limiting enzyme for glycolysis?
A
Phosphofructokinase
6
Q
What is the substrate of the citric acid cycle?
A
Acetyl CoA
7
Q
What are the products of the citric acid cycle?
A
ATP, 3 NADH, 2 carbon dioxide, FADH2
8
Q
What is the rate limiting enzyme of the citric acid cycle?
A
Isocitrate dehydrogenase
9
Q
Where in the cell & under what conditions (aerobic or anaerobic) does the ATP-CP System operate?
A
In the cytosol – anaerobic
10
Q
Where in the cell & under what conditions (aerobic or anaerobic) does Glycolysis operate?
A
In the cytosol – anaerobic
11
Q
Where in the cell & under what conditions (aerobic or anaerobic) does the Citric Acid Cycle operate?
A
In the mitochondrial matrix – aerobic
12
Q
Where in the cell & under what conditions (aerobic or anaerobic) does the Electron Transport System operate?
A
Within the mitochondria–aerobic
13
Q
What is produced or released for the energy pathway ATP-CP System?
A
ATP & Creatine
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)
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.
16
Q
What is produced or released for the energy pathway of the Electron Transport System?
A
26-28 ATP. 6 H2O.
17
Q
What is the time to fatigue for the ATP-CP System?
A
10 - 15 seconds.
18
Q
What is the time to fatigue for Glycolysis?
A
60 - 90 seconds.
19
Q
What is the time to fatigue for the Citric Acid Cycle?
A
A few hours.
20
Q
What is the time to fatigue for the Electron Transport System?
A
A few hours.
21
Q
What is the rate-limiting enzyme for the Citric Acid Cycle?
A
Isocitrate dehydrogenase.
22
Q
What is the rate-limiting enzyme for the Electron Transport System?
A
Cytochrome oxidase.
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.
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.
25
What is a stimulus?
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.)
26
What is a sensor?
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
27
What is the integrating center?
- 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
28
What is an effector?
- 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
29
What are the substrates of the electron transport system?
Hydrogen ions, high-energy electrons (from NADH and FADH2)
30
What is the effector's action?
The effector is an anatomical structure
EXAMPLES:
> sweat gland secreting sweat
> specific muscle contracting
31
What is a response?
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.
32
What are the components of an atom? Which are located in the nucleus? Where do the e- exist?
Protons (+), electrons (-), and neutrons (no charge). N+P = in the nucleus. E- exist in orbitals or shells.
33
What are the major essential elements for life?
C, H, O, N, P, Ca, Na, K, Cl, S, Mg
34
What are the minor or trace essential elements?
Selenium, molybdenum, manganese, chromium, iodine
35
--> atomic number 7
--> chemical sym. N
--> atomic weight 13
What does the atomic number tell you?
OF PROTONS IN AN ATOM. And therefore what atom it is.
36
--> atomic number 7
--> chemical sym. N
--> atomic weight 13
What does the atomic mass or weight tell you?
The sum of N+P in an atom. Units of measurement = 1 atomic mass unit (amu)
37
What are isotopes?
Variations of an element that differ in mass. Same # of protons, but neutrons vary
38
What are ions?
Charged atoms
39
What are cations?
Positively charged ions (+)... LOST electrons
40
What are anions?
Negative charged (-)...GAINED electrons
41
Name 4 things electrons can do?
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.
42
Describe 4 types of chemical bonds?
1. Covalent (strong)
2. Ionic
3. Hydrogen (weak)
4. Van der Waals forces (very weak)
43
What is the name of the bond between two monosaccharides?
A glycosidic bond
44
What makes a covalent bond "nonpolar?"
Electrons shared **equally** between atoms
45
What is the name of the bond that connects glycerol to fatty acids?
Ester bonds
46
What makes a covalent bond "polar"?
One atom in the molecule has
| stronger pull on the shared electrons
47
What is an ionic bond?
Transfer of an electron(s) from one atom to
| another, like in NaCl
48
What are some common cations in physiology?
Na+, K+, Ca2+, H+, Mg2+
49
What are some common anions in physiology?
Cl-, HCO3- (bicarbonate), HPO4,2- (phosphate) & SO4,2- (sulfate)
50
This kind of bond readily breaks in an aqueous environment.
Hydrogen bond
51
This bond is the strongest in an aqueous
| environment, often needing enzymes or high temperatures to be broken.
Covalent bonds
52
This weak bond can form between any two
| atoms, as long as their nuclei are close enough.
Van der Waals forces
53
This bond typically exists between polar
| covalent molecules, like water.
Ionic bonds
54
What is the normal pH range for human blood? Is it neutral, acidic, or basic?
7.35 to 7.45, with the average at 7.40.
55
What is the role of buffers? What is the primary buffer in human blood?
Buffers minimize changes of pH. Bicarbonate ion (HCO3-).
56
What is a biomolecule? Also, name all 4.
```
Biomolecules are a subset of
organic molecules that are
important in living organisms.
1. Carbohydrates.
2. Lipids.
3. Nucleotides/nucleic acids
4. Proteins
```
57
What is the simplest form or unit of a biomolecule? What is it's nickname as well?
A MONOMER!!! "Building-blocks"
58
Define a polymer.
Chain of two or more biomolecule monomers
59
What is the most abundant biomolecule?
Carbohydrates
60
What is the monomer (also called simple sugars) of carbohydrates?
```
Monosaccharides.
EXAMPLES:
> Glucose
> Fructose
> Ribose
```
61
What is the polymer (also called "complex carbohydrates") of Carbohydrates?
Polysaccharides.
EXAMPLES:
> Glycogen – storage form of carbohydrates in animals
> Starch – storage form of carbohydrates in plants
> Cellulose – dietary fiber, non-digestible by humans
62
What is the name of the bond that links individual nucleotide monomers to nucleic acid polymers?
phosphodiester bonds
63
What is the intermediate level of Carbohydrates?
> Disaccharides: Made up of 2 monosaccharides
| > Oligosaccharides: Made up of a few (e.g., 3 - 10) monosaccharides
64
What is the name of the bond between two monosaccharides?
A glycosidic bond
65
What is the monomer of Lipids?
Fatty acids.
| > Can be saturated or unsaturated
66
What is the polymer of lipids?
Monoglycerides, diglycerides, and triglycerides.
67
What are nucleotides and their function?
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
What are the 5 nitrogenous bases in nucleotides?
A denine
T hymine (in DNA only, instead of Uracil)
G uanine
C ytosine
U racil (in RNA only, instead of Thymine)
69
What is the name of the bond between individual amino acids?
A peptide bond
70
Which monosaccharides are used in nucleotides?
Deoxyribose (in DNA)
| Ribose (in RNA)
71
What is the polymer of nucleotides/nucleic acids?
DNA & RNA
72
What is the monomer for Proteins? (The workers of your cells, and most versatile biomolecule)
Amino acids (AAs) = building blocks of all proteins. 9 essential, 11 non essential.
73
What are the 5 polymers for proteins called?
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
Describe the PRIMARY level of protein organization.
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
Describe the secondary level structures that emerge when nearby amino acids chemically interact.
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
Describe the tertiary level of protein organization.
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
Describe the quaternary level of protein organization.
```
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
Name some common factors that affect protein structure.
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
What are the three main body cavities (structural/ anatomical compartments)?
Cranial, thoracic, and abdominopelvic cavities
80
Fatty acids are the monomer form of
| what biomolecule category?
Lipids
81
This category of biomolecule carries out
diverse jobs within the cell, such as
energy storage, communication, and
information storage.
Nucleotides/nucleic acids.
82
Polymers in this biomolecule category
| have four levels of structural complexity.
Proteins
83
Sucrose and glucose are examples of this
| biomolecule category.
Carbohydrates
84
Steroid hormones are part of this
| biomolecule category.
Lipids
85
What are the 7 functional categories of proteins?
```
E nzymes
M embrane transporters
S ignal molecules
R eceptors
B inding proteins
I mmunoglobulins
R egulatory proteins
```
86
What is the lumen?
The interior space of hollow organs
87
What do enzymes do?
Catalyze (speed up) chemical reactions
88
What do membrane transporters two? What are the two types?
Move polar substances across cell membranes. Two types: channels or carrier proteins
89
what is the intracellular fluid?
fluid inside of the cell
90
What is an example of signal molecules?
Hormones or neuropeptides
91
What is the role of receptors?
Bind signaling molecules. Trigger a change in cell function
92
What do binding proteins do? Name two examples.
Bind and transport nonpolar molecules around the body’s aqueous environment
Examples: hemoglobin, lipoproteins, etc.
93
What type of compartments are physiologists focused on?
Functional compartments
94
What is the alternate name for immunoglobulins? What are their role?
Also called antibodies. Involved in the immune response
95
What is the extracellular fluid?
Fluid outside of the cell
96
Role of regulatory proteins and what is their alternate name?
Regulate of gene expression and protein synthesis. Also called transcription factors
97
The molecule or ion that it binds is generally called a _________. Or a _______ if it binds to an enzyme or membrane transporter.
Ligand; substrate
98
Name and describe the several important principles of protein-ligand interactions.
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”
>> Some proteins are more specific (or limited) in what they can bind than others
99
What is protein modulation?
“Modulation” means to either increase or decrease the activity of a protein
100
What are the two types of extracellular fluid and where are they located?
Plasma - fluid in blood vessels
| Interstital fluid - surrounds most body tissue cells
101
What are some ways to modulate the action of cellular proteins?
Increase or decrease protein action
102
What are the protein modulators that INCREASE (activators) the action called? List all of their subtypes.
1. Proteolytic (lyse = break or rupture)
2. allosteric
3. **cofactors**
4. covalent
103
What are the four functions of the cell membrane?
A selectively permeable barrier; gateway for exchange between intra and extracellular compartments; communication from cell to cell; cell and tissue structure.
104
What are the protein modulators that DECREASE (inhibitors) the action called? List all of their subtypes.
1. Proteolytic
2. allosteric
3. **competitive**
4. covalent
105
What is covalent modulation?
Attachment of atoms or
functional groups to
modulate proteins
106
How would a protein cell avoid the problem of saturation?
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
This category of proteins can activate and
| inactivate genes, which will change the levels of protein workers in cells.
Regulatory proteins
108
What is the cell membrane composed of?
A phospholipid bilayer, cholesterol, and embedded proteins
109
These protein categories are involved in cell-to-cell communication. List them all.
Receptors, signal molecules, binding proteins.
110
Proteins in this category catalyze chemical
| reactions.
Enzymes
111
Molecules, especially nonpolar ones, are moved around the body by these types of proteins.
Binding Proteins.
112
What are the two general types of proteins contained in the cell membrane?
Integral proteins and peripheral proteins
113
Why do humans and other organisms need energy?
Energy is needed to do work
114
What kind of work does the body perform? List all 3.
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
WHO does the work of the cells?
Proteins, and they need a lot of ENERGY to do the work
116
What are the two types of integral proteins in the cell membrane, where are they located, and how are they removed from the membrane?
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
What are the two states of energy? Describe them.
1. Kinetic - energy in motion or action
| 2. Potential energy (free energy) - STORED energy
118
What is entropy?
All processes naturally move from state of order to disorder
119
ATP --> ADP + Pi + Energy is an example of....
An EXergonic chemical reaction, where free energy is released from
broken chemicals bond in the
reactant(s)
120
ADP + Pi + Energy --> ATP is an example of what chemical reaction?
ENDERgonic, where some of the activation energy is retained and added to the product’s free energy by creating new
chemical bonds
121
The energy to create new bonds often comes from one or more is called _______.
COUPLED REACTIONS
122
Where are peripheral proteins located and are they easily seperated from the cell membrane?
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
What is metabolism?
The sum of all energy exchanges in an organism
124
What are the two phases of metabolism?
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
What components of the cell membrane are considered “congugated”?
phospholipids
126
True or False: ATP is stored within the body.
FALSE. It only lasts - 5 seconds and must be replaced as quickly as itʼs used
127
ATP --> ADP + Pi + Energy is called...
This is called ATP hydrolysis. Energy then used for cellular work, some lost
as heat
128
What are the two anaerobic energy pathways?
ATP-CP System
| Glycolysis
129
Which molecules of the cell membrane have a polar and a nonpolar end?
phospholipids and cholesterol
130
True or false: anaerobic = doesn't require O2
TRUE
131
True or false: aerobic = requires O2
TRUE
132
What are the two aerobic energy pathways?
Citric Acid Cycle (Krebs Cycle)
| Electron Transport System
133
What proteins in the cell membrane are in direct contact with the intra- and extracellular compartments?
transmembrane proteins
134
True or False: All energy pathways are functioning all of the time.
True. One or two might be primary (or more active) depending
on the conditions, but the others still contribute to some
degree
135
Where do aerobic pathways take place?
In the mitochondria
136
Which end (polar or nonpolar) of a phospholipid faces the inside or the outside of the cell
The polar end
137
Where do anaerobic pathways take place?
In the cytosol.
138
Oxygen combines with H+ at the end of this pathway.
Electron Transport System.
139
Carbon dioxide is produced by this pathway.
Citric Acid Cycle
140
These pathways do not require oxygen.
ATP-CP System, Glycolysis
141
These pathways DO require oxygen.
Citric Acid/Krebs Cycle, Electron Transport System
142
NADH and FADH2 are oxidized in this pathway.
Electron Transport System
143
What are inclusions? Give some examples and a brief definition
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
What makes up the cytoskeleton?
Protein fiber inclusions. Such as microfilaments, intermediate fibers, and microtubules.
145
What is the function of the cytoskeleton?
Determines cell shape, internal organization, assembly of cells and tissues, cell membrane movement, and intracellular transport.
146
What is the function of motor proteins?
Move organelles and other structures around the cell by walking down the cytoskeleton as a road. Use energy from ATP to create movement. 
147
Why do membrane-bound organelles have membranes?
To enable protected chemical reactions.
148
What is the job of the mitochondria? What processes does it use.
Generates ATP for cell energy through aerobic processes. The powerhouse of the cell.
149
Difference between Rough ER and Smooth ER:
Rough ER: Ribosomes on external surface give the “rough”appearance
Smooth ER: Lipid and fatty acid synthesis
150
This cell structure is responsible for the synthesis of lipids:
SMOOTH ER
151
This cell structure is responsible for the synthesis of proteins:
Ribosomes
152
This cell structure is responsible for the packaging of proteins for transport
Golgi complex
153
This cell structure is responsible for the housing of genetic material of the cell
Nucleus
154
This cell structure is responsible for the site of aerobic respiration
Mitochondria
155
This cell structure is responsible for the post-translational modification of proteins
ROUGH ER
156
This cell structure is responsible for giving the cell structure and enables membrane movement
Cytoskeleton
157
This cell structure is filled with molecules for secretion or storage
Cytoplasmic vesicles
158
What are gap junctions?
Channels that connect cytoplasm of two adjacent cells
| > Permit chemical & electrical signals to pass from one cell to the next VERY QUICKLY
159
What are tight junctions?
As the name suggests, the restrict movement between adjacent cells
> Create barriers that help regulate movement of substances
160
What are desmosomes?
Button-like, anchoring junctions – help cells form strong tissues
161
What are the three things that make up nucleotides?
Nitrogenous bases, a 5-carbon sugar, and one or more phosphate groups
162
Which nitrogenous bases are purines?
Adenine and Guanine
163
Which nitrogenous bases have pyrimidine structures?
Cytosine
Thymine
Uracil
164
What forms the backbone of DNA and RNA?
Sugar-phosphate
165
Name 3 disaccharides and their monomers.
Sucrose - glucose + fructose
Maltose - glucose + glucose
Lactose - glucose + galactose
166
What are the two types of membrane transporter proteins?
channels
| carrier proteins
