Exam 1 Flashcards

1
Q

Heart, blood vessels, blood

A

circulatory

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2
Q

transports materials between all cells of the body

A

circulatory

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3
Q

stomach, intestine, liver, pancreas

A

digestive

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4
Q

conversion of food into particles that can be transported into the body; elimination of some wastes

A

digestive

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5
Q

thyroid gland, adrenal gland

A

endocrine

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6
Q

coordination of body function through synthesis and release of regulatory molecules

A

endocrine

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7
Q

thymus, spleen, lymph nodes

A

immune

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8
Q

defense against foreign invaders

A

immune

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9
Q

skin

A

integumentary

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10
Q

protection from external environment

A

integumentary

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11
Q

skeletal muscles, bone

A

musculoskeletal

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12
Q

support and movement

A

musculoskeletal

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13
Q

brain, spinal cord

A

nervous

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14
Q

coordination of body function through electrical signals and release of regulatory molecules

A

nervous

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15
Q

ovaries and uterus, testes

A

reproductive

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16
Q

perpetuation of the species

A

reproductive

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17
Q

lungs and airways

A

respiratory

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18
Q

exchange of oxygen and carbon dioxide between the internal and external enviornments

A

respiratory

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19
Q

kidneys, bladder

A

urinary

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20
Q

maintenance of water and solutes in the internal environment; waste removal

A

urinary

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21
Q

what approach do most physiologists take to study physiological processes

A

mechanistic approach

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22
Q

the approach that is “bench to bedside”

A

translational research

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23
Q

five major themes

A
  1. Structure and function across all levels of organization
  2. energy transfer, storage, and use
    3.information flow, storage, and use within single organisms and within a species of organism
  3. homeostasis and the control systems that maintain it
  4. evolution
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24
Q

study of body functions in a disease state

A

pathophysiology

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25
volume of blood cleared of substance x per unit of time
Clearance
26
is clearance a direct or indirect measure of how substance x is handled by the body
Indirect
27
Hepatocytes
Liver cells
28
body compartments is relatively stable (NOT equal) and there is no net movement of material between two compartments
Steady States
29
what are the two control systems
local control and long-distance reflex control
30
Three components of control systems
input signal -> a controller (integrating center) ->output signal that creates a response
31
integrates incoming information and initiates an appropriate response
integrating center
32
What is different about long-distance reflex
more complex and might include multiple sources and have an output that acts on multiple targets
33
Contain carbon, oxygen, and hydrogen
biomolecules
34
4 main groups of biomolecules
-carbohydrates -lipids -proteins -nucleotides
35
conjugated proteins are..
protein combines with other biomolecule
36
Glycosylated molecules are
carbs attached to other biomolecules
37
Lipid characteristics
-nonpolar -hydrophobic
38
what does the lipid structure consist of?
-glycerol backbone -fatty acids attached
39
Difference between saturated and unsaturated fatty acids
unsaturated fatty acids has at least one carbon to carbon double bond while saturated fatty acids only have single bonds between carbons
40
Elconsanoids
-immune system functions
41
Steroids
-four linked carbon ring -Cholesterol is the primary source of steroids in the body
42
Cortisol is a example of a
steroid
43
phospholipids
-a lipid structure attached to a phosphate group -Amphipathic
44
What two lipids are components of animal cell membranes
Cholesterol and phospholipids
45
Monosaccharides, disaccharides, and polysaccharides are all...
Carbohydrates
46
2 or more Amino Acids bound is a
peptide
47
what type of bond binds two or more Amino Acids together
Peptide Bond
48
2-9 Amino Acids
Oligopeptides
49
10-100 amino acids
polypeptides
50
>100 amino acids
Proteins
51
What happens in the primary Structure of peptides and proteins
20 protein forming amino acids assemble into polymers called peptides
52
what happens in the secondary structure of peptides and proteins
covalent bonds angles between amino acids determine the structure of the peptides
53
what are the two primary structures
-alpha helix -beta strands form sheets
54
What happens in the tertiary structure of proteins
-proteins takes a three dimensional shape --either chains or globular proteins
55
What happens in the Quaternary Structure of proteins
the subunits (globular proteins) combine with noncovalent bonds
56
what is produced when a peptide bond is formed
water
57
electrons shared between atoms
covalent bonding
58
gain/loss of electrons
ion formation
59
capture and transfer of energy (ATP synthesis)
high energy electrons
60
Unpaired electrons
free radical
61
what are important cations of the body
sodium, potassium, calcium, hydrogen
62
what are important anions of the body
Chloride and Bicarbonate
63
Are polar or non polar molecules soluble in aqueous sol
polar
64
Weak, nonspecific interactions
wanderwaals forces
65
weak bonds occurring between hydrogen, oxygen, florine, nitrogen
Hydrogen Bonds
66
Electrostatic interactions between cations and anions
Ionic bonds
67
polar molecules dissolve easily
hydrophilic
68
non polar do not readily dissolve
hydrophobic
69
Donate H+
Acids
70
Accepts H+
Bases
71
What is the equation to measure pH
pH=-log [H+}
72
The seven categories of soluble proteins
-enzymes -membrane transport -signaling Molecules -binding proteins -immunoglobulins -regulatory proteins
73
Molecule that binds to the binding sit on another molecule
Ligand
74
What do binding properties dictate
interactions and responses
75
High affinity means
more likely for the protein and ligand to bind
76
for reactions at equilibrium, the ratio of reactants and products are the same
Law of mass action
77
what does K_d
dissociation constant
78
high affinity means
low K_d
79
functionally and structurally similar proteins
isoforms
80
do some proteins need to be activated?
Yes
81
-reverse antagonists that compete with the ligand -agonists can also compete, but would have the same effect/response
Competitive Inhibitors
82
-bind to different site -can be agonists or antagonists
Allosteric Modulators
83
What physical factors can denature proteins
Tempt and pH