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anatomy 1 exam Flashcards

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1
Q

homeostasis

A

the existence of a stable internal environment.
Maintaining homeostasis is vital to maintaining proper physiological
function and thus crucial for survival.

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2
Q

why is it important to maintain homeostasis?

A

Organisms (including humans) live in changing and unpredictable
environments.
By maintaining homeostasis (constant internal environment),
physiological functions can proceed in a constant environment and
avoid disruption from environmental influences.

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3
Q

Differentiate between the study of anatomy and the study of physiology.

A

-Anatomy refers to the internal and external structures of the body and their physical relationships,

  • physiology refers to the study of the functions of those structures.
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4
Q

autoregulation.

A

When a cell, tissue, organ, or
organ system adjusts in response to an environmental
change. Does not involve the nervous or endocrine
systems.
System regulates itself.

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5
Q

Extrinsic regulation

A

Results from activities of the
nervous system or endocrine
system detecting a change in the
environment and sending
electrical/chemical signal to adjust
activities of another system.
Extrinsic = operating from outside.
Example:
Your nervous system detects a
drop in environmental temperature
and sends signal to muscles to
increase heat production.

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6
Q

difference between auto and extrinisc regulation

A

auto
- small scale
-system regulates itself
- no nervous and endocrine system

extrinsic
-larger scale
- nervous or endocrine system

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6
Q

negative feedback

A

Negative feedback opposes
variations from normal (set point).
Most feedback mechanisms in
human body are negative.

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7
Q

homeostatic regulation

A

Receptor- detects environmental stimulus
control center- receives and processes the information by keeping a set point
effector- Cell or Organ that responds to control center’s
commands.

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8
Q

positive feedback

A

Positive feedback mechanisms
produce a response that
enhances the original homeostatic
change.
Much less common than negative
feedback mechanisms.

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9
Q

neg feedback

A

response to the change occurs in real time not over a long period of time. Body immidiatly tries to correct error

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10
Q

matter

A

anything that takes up space.

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11
Q

mass

A

the amount of material in
matter (not the same as weight).

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12
Q

volume

A

the amount of space That matter occupies.

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13
Q

what are atoms composed of

A

subatomical particles
- protons +
- electrons -
neutrons =

Electrons orbit nucleus in ELECTRON CLOUD.
The number of protons is generally equal to the number of
electrons (results in neutrally charged atom)

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14
Q

atomic number

A

The number of protons in
the nucleus of an atom

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15
Q

atomic mass

A

Roughly equal to the
number of protons +
number of neutrons in
nucleus of atom.
Remember: #protons = # neutrons in neutrally charged atom.
For Carbon….Atomic mass = 6 protons + 6 neutrons = 12

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16
Q

element

A

a pure substance composed of only one
type of atom.

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17
Q

isotopes

A

atoms of same element that contain
different number of neutrons.
Does not change charge, but does change
atomic mass.

  • Thats why the atomic mass of Carbon is not exactly 12
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18
Q

Radioisotopes

A

isotopes with unstable nuclei that break down and
give off subatomic particles or radiation.
Uses:
Cancer Treatments
Tracers/labeling
Imaging
Medical Diagnostics
Images
(top)

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19
Q

electron orbit, cloud, energy levels

A

Electrons travel around the
nucleus in defined orbits.
The area that electrons orbit
within is called the electron
cloud.
Within an electron cloud,
electrons occupy an
orderly series of energy levels

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20
Q

orbital energy levels

A

E1 – lowest energy level.
Can hold up to 2 electrons.
E2 – Can hold up to 8
electrons.
E3 – Can hold up to 8
electrons.
E1 fills before electrons
occupy E2, and so on.

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21
Q

valence shell
valence electrons

A

outermost energy level of atom
- what the valence shell contains is valence electrons

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22
Q

molecules

A

Any chemical structure
consisting of atoms held
together by shared
electrons.

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23
Q

compounds

A

pure chemical substance
made up of atoms of two
or more different
elements in fixed
proportions

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24
molecular weight
the sum of the atomic weights of a molecules components.
25
ionic bonds
chemical bonds formed by the electrical attraction Between negatively and positively charged ions. Ionic bonds are weak (held together only by electrical charges attracting)
26
covalent bond
chemical bonds formed by atoms sharing electrons in outer most energy level. Shared electrons orbit both nuclei Covalent bonds are strong because the atoms share electrons
27
Polar covalent bond and nonpolar
Electrons are shared unequally. * Electron spends more time orbiting one atom. * Result is one atom has slightly negative charge while other has slightly positive charge. Non-polar * Electrons are shared equally by both atoms. * Electron spends equal time orbiting both nuclei.
28
Rank bonds from weak to strong (1,2,3)
1 Hydrogen bonds the weakest 2 ionic bonds stronger than hydrogen bonding 3 covalent bonds are the strongest
29
synthesis reaction
increasing the number of bonds (anabolism)... Building more complex molecules from smaller pieces. So the number of bonds increases
30
decomposition reaction
catabolism... Breaking down larger molecules into smaller pieces. So the number of bonds decreases
31
exchange reaction
shuffling components of molecules pairing decomposition with synthesis
32
hydrolysis reaction
decomposition reaction involving water as a reactant
33
Anabolism
2. Anabolism is the process of building up complex macromolecules, such as nucleic acids, proteins, polysaccharides, and lipids.
34
catabolism
Catabolism is the process of breaking down complex macromolecules into simple molecules, such as carbon dioxide, water, and ammonia.
35
work
The movement of an object or change in physical structure of matter.
36
physiological work
Any process that increases order and requires energy. Examples: building proteins from amino acids, transporting solutes across cell membranes.
37
kinetic vs potential energy
kinetic- energy that can be transferred to another object to do work potential- energy that has the potential to do work
38
Atp
main form of cellular energy. Breakdown of ATP to ADP releases large amounts of energy that can be used by cells to perform physiological work.
39
Hydrolysis
decomposition involving water. Reversal of dehydration synthesis water is added between two molecules whic is what breaks molecules apart
40
Dehydration reactions
formulation of complex molecules by the removal of water. two molecules are joined by removal of water
41
exergonic reaction
Reactions that result in the net release of energy. Relatively common in the body. They generate the heat that maintains your body temperature.
42
endergonic reaction
Endergonic Reactions Reactions that result in the net absorption of energy. Examples: the synthesis of fats and proteins.
43
activation energy
the amount of energy needed to start a reaction. Methods of Activating Reactions 1. Temperature changes 2. pH changes 3. Enzymes (methods 1&2 above would be deadly to cells)
44
enzymes
promote chemical reactions by lowering the activation energy required to begin the reactions. Enzymes belong to class of substances called catalysts. Enzymes make it possible for chemical reactions to take place under normal conditions of cells.
45
important enzyme facts
IMPORTANT!!! Enzymes affect only the rate at which reactions occur. Enzymes do not affect the direction that reactions progress or the products formed. Enzymes are proteins.
46
active site
a groove or pocket in which one or more substrates can fit. Substrates fit into active site like a “lock and key” based on shape and charge. Enzymes fit only specific substrates (Also known as “SPECIFICITY”).
47
saturation limit
the substrate concentration required to have the maximum rate of reaction.
48
inert have
1) biologically important atoms 2) reactivity 3) abundance
49
organic compounds
contain C,H
50
inorganic
dont contain C,H as primary structures may syill contain them
50
organic compounds examples
Common Examples: * Methane * Sugars (glucose C6H12O6) * Lipids * Proteins
50
inorganic compounds examples
Important inorganic compounds in human body: * Carbon dioxide (CO2) * Oxygen (O2) * Water (H2O)
50
read pt 2
Some organic molecules contain polar covalent bonds, which attract water molecules and form hydration spheres (see image to the right). These are referred to as hydrophillic (water loving). Other organic molecules have no polar covalent bonds and do not form hydration spheres. These are referred to as hydrophobic (water fearing).
51
suspension
Contains large molecules in solution, but if undisturbed, its particles will settle out of solution due to gravity. * Example: blood
51
read
Many inorganic compounds are held together by ionic bonds. When they come in contact with negative and positive ends of water molecules, these compounds dissociate (break apart). Dissociated ions are surrounded by water molecules forming hydration spheres. The result is an aqueous solution.
51
colloid
A solution containing dispersed proteins or other large molecules. * Particles will remain in solution indefinitely
51
Why is water good solvent?
Polar covalent bonding of H and O in water molecules creates positive and negative ends (poles).
51
heat capacity
the quantity of heat required to raise the temperature of a unit of mass of a substance 1°C.
51
why does water have a high heat capacity?
Water has a high heat capacity because of hydrogen bonding among molecules.
52
lubrication
Because there is little friction between water molecules, water is an effective lubricant
53
salt
an ionic compound that contains any cation (except H+) and any anion (except OH-) Salts are held together by ionic bonds and dissociate in water. Salts are neutral (do not effect pH)
54
carbohydrate
an organic molecule that contains C, H, and O in a ratio near 1:2:1 Carbohydrates are: 1. generally water soluble. 2. most important as energy sources that are catabolized.
55
monosaccharides
Monosaccharides (simple sugars) are carbohydrates with three to seven carbon atoms.
56
Disaccharides
two monosaccharides joined together. Have a sweet taste and are soluble in water
57
Polysaccharides
complex carbohydrates formed when repeated dehydration synthesis reactions add additional mono or disaccharides. Can be straight chain or highly branched in structure.
58
starches
large polysaccharides formed from glucose molecules.
59
lipids
contain C, H, and O. C:H is near 1:2. Contain much less O than carbohydrates. Most lipids are insoluble in water. Lipids form essential structural components of all cells. Lipid deposits in the body are important sources of energy reserves. Lipids provide (on average) twice as much energy as carbohydrates do.
60
fatty acids
long C chains with H atoms attached. A carboxyl group (-COOH) is always attached to one end of a fatty acid.
61
saturated or unsaturated fatty acids
- in saturated each C atom in tail has four single covalent bonds. - in unsaturated one or more of the single bonds is replaced by a double covalent bond.
62
steroids
large lipid molecules with a distinctive four-ring C structure.
63
proteins
The most abundant (and most important) organic molecules in the body.  Proteins account for ~20% of total body weight.  Contain C, H, O, and N  Proteins are made up of Amino Acids.
64
7 functions of proteins
1. Support (structural proteins) 2. Movement (contractile proteins) 3. Transport (transport proteins) 4. Buffering pH 5. Metabolic Regulation (enzymes) 6. Coordination & Control (hormones) 7. Defense (antibodies, clotting proteins)
65
protein primary structure
The primary structure of proteins is the sequence of amino acids along the length of a single polypeptide. Primary structure is determined by peptide bonds
66
protein secondary structure
The secondary structure is the result of hydrogen bonding between atoms at different parts of the polypeptide chain. Secondary structure can be either an alpha helix or beta sheet.
67
protein tertiary structure (3)
The tertiary structure is the complex coiling/folding that gives the protein its final 3D shape
68
protein quatenary structure
The quaternary structure is the interaction among individual polypeptides to form a protein complex. A single polypeptide (left) interacts with other polypeptides to form a large protein molecule (right) Tertiary Structure Quaternary Structure
69
nucleic acids
large organic molecules made of C, H, O, N, and P -Nucleic acids consist of one or two long chains of nucleotides bound together by dehydration synthesis. Purines = double-ringed Pyrimidines = single-ringed
70
DNA
consists of a pair of nucleotide chains held together by hydrogen bonds.
71
Rna
consists of a single chain of nucleotides. Shape of RNA depends on the order of nucleotides in RNA chain and the interactions among them

anatomy (11 decks)

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