Unit One: Lecture 1,2,3 Flashcards

1
Q

Anatomy and physiology, come from the root words?

A

“Ana”=up/open, “tomy”=to cut

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2
Q

Anatomy=? Learning the…

A

=Structure! Parts what they are made of, where parts are located, physical relationships between different structures.

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3
Q

Physiology=? Study of…

A

=Function! How living organisms perform their functions.

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4
Q

Levels of study.

A

Cell
Organ
System

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5
Q

Change in blank causes change in blank?

A

Change in structure causes change in function.

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6
Q

Tumors in organs along GI tract, what would you expect?

A

Cause a blockage, unable to poop.

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7
Q

Homeostasis was formed from the words?

A

“Homeo”, and “stasis”.

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8
Q

Homeostasis regulation:

A

Adjusting physiological processes in response to changes in the external environment.

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9
Q

Homeostatic Regulatory Mechanism:

A

Receptor=input
Control center=processes information
Effector=responds to commands from the control center

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10
Q

Why do our bodies perform homeostasis?

A

Our body likes to be just right. Ex. Temperature, amount of red or white blood cells, and infection.

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11
Q

Receptor:
Control center:
Effector:

A

:see’s that something has changed
:processes information, sends command to the effector
:gets command from control center to affect a change
*receptors constantly communicating with brain, how we know when its hot.

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12
Q

Blood vessels blank when too hot, and blank when too cold.

A

Blood vessels expand (dilate) vessels close to surface so it is able to cool off ( why you turn red when hot), blood vessels constrict to keep blood warm ( why you turn blue or pale when cold)

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13
Q

Most feedback loops in the body are…?

A

Negative, very few feedback loops are positive.

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14
Q

Positive feedback loop…

A

Leads to exaggeration of original stimulus, escalating cycle:can speed up a dangerous process, ex. Blood clotting after a laceration, positive feedback is rare.

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15
Q

Negative feedback loops…

A

Goal is to keep the body happy aka maintain homeostasis, a good example would be temperature regulation (temperature sensors in skin send a message to the brain that the body is hot and the brain sends commands to the effectors also known as the sweat glands in this example and then causes temperature to return to normal levels, if too cold the body will shiver its always reverses)

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16
Q

Describe the structure of an atom and the arrangement of the electrons.

A

An atom has a nucleus with an electron cloud around the nucleus, proton and neutrons are found in the nucleus and the electrons are found moving around the nucleus. Electrons are arranged into shells the first shell fits 2, then 8, then 18 but is stable with 8.
2-8-8

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17
Q

Ionic bonds

A

One atom donates an electron becomes a cation, one atom accepts the electron becomes a anion. (Can tell its ionic if there are charges/ ions, between metals and nonmetals.)

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18
Q

Covalent bonds

A

Atoms share pair of electrons( they share the electrons to fill electron shells, want 8 electrons in outer most shell or valance shell).
Single covalent bond=one pair of shared electrons.
Double covalent bond= two pairs of shared electrons.
Triple covalent bond= 3 pairs of shared electrons.
Between two nonmetals.

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19
Q

Nonpolar covalent bonds vs polar covalent bonds

A

Nonpolar- equal sharing of electrons between atoms that have equal pull on the electrons.
Polar- unequal sharing of electrons because one atom has disproportionately strong pull on the electrons.

20
Q

Hydrogen bonds

A

Form between molecules based on electrical attraction (WEAK POLAR BONDS), attraction between a slight positive and a slight negative charge (what causes h2o to have surface tension).

21
Q

Decomposition reaction (catabolism)

A

Breaks chemical bonds, exergonic reactions, release energy(ex breaking down food to use energy contained within). AB—>A+B.

22
Q

Synthesis reaction (anabolism)

A

Forms chemical bonds, endergonic reactions, require input of energy from another source(ex photosynthesis requires solar energy). A+B—>AB.

23
Q

Activation energy

A

Is the amount of energy needed to start a reaction

24
Q

Enzymes

A

Are protein catalysts that lower the activation energy of reactions.

25
Q

Describe activation energy and the basic functions of enzymes

A

Activation energy is the amount of energy required to start a reaction, enzymes are catalysts that speed up chemical reactions without themselves being permanently changed or consumed. Enzymes lower the activation energy.

26
Q

Describe the structure and properties of water

A

All can be applied to blood:chemical properties;1.solubility-molecules dissolve in water 2.reactivity-chemical reactions take place in water 3.high heat capacity- takes a lot of energy to raise temperature 4. Lubrication- low friction between molecules. Essential to all physiological systems. STRUCTURE- 2 slightly positive hydrogen atoms and one slightly negative oxygen atom. Polar covalent bond !

27
Q

Ph is essentially…

A

A scale from 0-14 that shows the amount of H+ ions present. ( pH-potential of H) #of hydrogen ions increase when an acid is added, #of hydrogen ions decrease when base is added.

28
Q

Acid

A

Hydrogen ion donor (#of hydrogen ions increases in water when acid is added)

29
Q

Base

A

(Alkali) hydrogen ion acceptor #of hydrogen ions decreases in water when base is added

30
Q

A pH of 5 is blank times more acidic than 7

A

100 times

31
Q

Organic molecule defined

A

Carbon, hydrogen, and usually oxygen.
Carbohydrates, lipids, proteins, nucleic acids(DNA,RNA).

32
Q

Explain the relationship between monomers and polymers.

A

Carbohydrates, lipids, proteins, and nucleic acids are made up of monomer subunits. Identical monomers(molecules) join together to form a polymer.

33
Q

Dehydration synthesis

A

Creation of larger molecules from smaller monomers where a water molecule is released.

34
Q

Hydrolysis

A

Chemical reaction in which a molecule of water breaks one or more chemical bonds. (Think water breaking).

35
Q

Structure and function of monosaccharides

A

Simple sugars that can be used by cells. glucose, fructose, galactose. Glucose most important source of energy. Most common structure is the ring form (c6h12o6).

36
Q

Structure and function of disaccharides

A

Formed by the union of two monosaccharides (reaction=dehydration synthesis). Examples sucrose, lactose. Energy source broken down prior to use. Structure is usually ring format, two monosaccharides joined usually by oxygen.

37
Q

Structure and function of polysaccharides

A

Many monosaccharides joined by dehydration synthesis. Examples glycogen, starch, cellulose. (Glycogen=glucose polymer, stored in skeletal muscles and liver. Storage of energy-needs to be broken down prior to use.

38
Q

Structure and function of fatty acids

A

Lipid monomers, hydrocarbon chain with carboxyl (COOH) group at the end.

39
Q

Structure and function of glycerides

A

Fatty acids attached to a glycerol molecule. Monoglyceride=1 fatty acid attached to glycerol. Diglyceride=2 fatty acids attatched to glycerol. Triglyceride=3 fatty acids attached to glycerol( how we store fatty acids made by dehydration synthesis.

40
Q

Structure and function of steroids

A

Lipids with a four ring hydrocarbon structure. (Cholesterol-steroid that forms basis for all other steroids)

41
Q

Protein structure (4 levels of structural complexity)

A

2 basic types of proteins by structure; 1.)fibrous proteins- long rope like strands add strength and durability to structures. 2.)globular proteins-spherical or globe like, function as enzymes, hormones, and other cell messengers. Proteins are most abundant organic molecules. *4 levels of structural complexity= 1:primary structure-amino acid sequence, 2:secondary structure-one or more segments of primary structure folded in specific ways(held together by hydrogen bonds), 3:tertiary structure-three-dimensional shape of peptide chain(twists, folds, and coils, including secondary structure);stabilized by hydrogen bonding, 4:quaternary structure-linking together two or more tertiary structures in specific arrangement; critical to function of protein

42
Q

How protein structure can be disrupted by denaturation

A

Destroying proteins shape by heat, pH changes, or exposure to chemicals. Disrupts hydrogen bonding and ionic interactions that stabilize structure and function. Denaturing=change in tertiary or quaternary structure makes protein nonfunctional.

43
Q

Primary functions of proteins in the body

A

1.support(structural proteins)
2.movement(contractile proteins in muscles)
3.transport proteins
4.buffers(regulate pH)
5.metabolic regulation
6.coordination and control(hormones)
7.defense(antibodies)

44
Q

How does the structure of an enzyme relate to its function

A

Enzymes are a protein and have a very specific shape, like proteins when put through intense conditions the shape is changed. This change in shape for enzymes causes a change in the function as now that enzyme can no longer bind to substrate as the unique shape has been altered.

45
Q

Describe the structure and function of DNA

A

Composed of two long chains that twist around each other to form double helix. Contains genes- recipe code for protein synthesis( process to make every protein ). Pentose sugar deoxyribose forms backbone of strand alternates with phosphate group. Bases A,G,C,T. Double helix half Oglethorpe by hydrogen bonding

46
Q

Describe the structure and function of RNA

A

Single strand of nucleotides; critical to making proteins, RNA contains pentose sugar ribose, RNA contains uracil instead of thymine. DNA can’t leave the nucleus that’s why we need RNA.

47
Q

Describe the structure and function of ATP

A

Cells use the energy from broken down food to produce ATP. ATP=energy storing molecule most important energy storage in cells. Adenosine triphosphate(ATP) adenine attached to ribose and 3 phosphate groups, main source of chemical energy in body.