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Integrative Physiology > Lecture 2 > Flashcards

Lecture 2 Flashcards

1
Q

Acids

A

Contributes H+ to solution

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2
Q

Bases

A

Decrease H+ in solution

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3
Q

Buffers

A

Minimize changes in pH of a solution

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4
Q

pH

A

-log[H+], scale ranges from 0 (most acidic) to 14 (most basic)

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5
Q

Law of mass action

A

For reversible reactions –> high concentration of products drives reaction towards more reactants, high concentration reactants drives reaction towards more products

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6
Q

How are functional groups important to physiology?

A

Functional groups change mol. shape/formula, shape influences function, can help form new bonds

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7
Q

Types of biomolecules

A

Carbohydrates, lipids, proteins, nucleotides/nucleic acids

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8
Q

Carbohydrates

A

Most abundant, can be simple (mono-) or complex (poly-)

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9
Q

Formula for carbohydrates

A

Carbon, hydrogen, oxygen- CnH2nOn –> carbon and oxygen will always be the same, hydrogens doubled

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10
Q

Carbohydrates provide

A

Quick energy

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11
Q

Difference between carbohydrate and hydrocarbon

A

Molecular formula - carbs follow the CnH2nOn formula

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12
Q

Lipids

A

Carbon and hydrogen, very structurally diverse

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13
Q

Diversity of Lipids

A

Eicosanoids, steriods, phospholipids, triglycerides (glyerol, fatty acid chains)

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14
Q

Saturated vs. unsaturated lipids

A

Saturated= saturated with hydrogens (single bonds only); ex. butter
Unsaturated= contains a double or triple bond; ex. junk foods

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15
Q

Result of inability to breakdown triglycerides

A

Digestion and absorption issues, vitamin deficiencies

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16
Q

Phospholipids

A

Addition of a phosphate group to a glyceride, makes molecule polar; generates phospholipid bilayer membranes –> phosphate side is polar end (hydrophilic)

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17
Q

How many amino acids are there?

A

20

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18
Q

Proteins

A

Enzymes, comprised of amino acids, four levels of structure, most versatile

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19
Q

Protein bonding

A

Disulfide bonds, hydrogen bonds, van der waals forces, ionic bonds/repulsions (all create unique protein shape

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20
Q

What are the layers of protein structure

A

Primary, secondary, tertiary, quaternary

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21
Q

Function of R group in amino acid backbone

A

Impacts different abilities/function/complexity to what amino acids/proteins can do

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22
Q

Sequence of amino acids

A

Generates different functions of proteins

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23
Q

What changes the 3D structure of proteins and influences shape and function?

A

R groups in amino acids, amino acid chain order, folding (bond interactions) –> adds to properties

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24
Q

Denatured proteins/enzymes

A

Heat, pH, changed location/solvent –> broken down quaternary, tertiary, secondary structure of proteins (primary structure remains in most occasions, unless strong acid)

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25
Q

Polymer formation

A

Dehydration synthesis (removal of water to connect peptide chains)

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26
Q

Primary protein structure

A

Sequence of amino acids; influences interactions in secondary sequence

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27
Q

Secondary protein structure

A

Alpha-helix, beta-pleated sheets

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28
Q

Quaternary protein structure

A

Fibrous proteins, globular proteins; contains subunits

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29
Q

Protein bonding

A

Hydrogen bonds, van der waals forces, ionic bonds, ionic repulsions, disulfide bonds –> all generate unique protein structure

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30
Q

In order for an enzyme to work, it must be

A

Soluble

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31
Q

How are protein interactions modulated?

A

Specificity, affinity (proteins are selective about bonding/binding)

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32
Q

Isoforms

A

Functionally similar proteins, encoded by similar genetics but not identical

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33
Q

Protein interactions

A

Binding, selectivity, molecular complementarity (specificity, affinity), isoforms

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34
Q

Selective protein binding

A

Induced-fit model (lock and key mechanism); use of binding sites –> cofactors and inhibitors can alter binding sites/bindings

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35
Q

Allosteric activation/inhibition

A

Changes conformation of protein to allow or inhibit interaction with ligand

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36
Q

Influence of pH and temperature on protein

A

Alter 3D shape of protein by disrupting hydrogen or S-S bonds, may be irreversible if protein denatures

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37
Q

Physical factors that affect protein function

A

Temp, pH, concentration of protein (up and down regulation), concentration of ligands, maximum reaction rate (saturation) –> availability of necessary components

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38
Q

Rate of protein activity

A

Maximal activity at certain temp, pH (optimal range) –> range of rates with varied temps, pH, etc.

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39
Q

Nucleotides and Nucleic acids

A

Comprised of base, sugar, phosphate; transmit and store information (DNA, RNA), transmit and store energy (ATP, cAMP, NAD, FAD)

40
Q

Types of extracellular fluids (2)

A

Plasma, interstitial fluids

41
Q

Functional compartments of the body

A

Extracellular (plasma, interstitial fluid) and intracellular fluid

42
Q

Interstitial fluid

A

Fluid between the circulatory system and cells

43
Q

Difference between extracellular and intracellular fluid

A

Intracellular - cytoplasm, extracellular - fluid outside cells, fluid in blood

44
Q

Homeostatic difference between extracellular and intracellular fluid

A

Difference in charge, chemicals, between fluids but differences ARE homeostatic

45
Q

Fluid mosaic model of a membrane

A

Phospholipid bilayer, membrane contains variety of other proteins, carbohydrates (glycoproteins), cholesterol

46
Q

Cell membrane functions

A
  1. physical barrier
  2. gateway for exchange (between intracellular and extracellular compartments)
  3. communication (cell membrane proteins)
  4. cell structure - intracellular and extracellular matrix
47
Q

Cell membrane protein types

A

Integral, peripheral, lipid-anchored

48
Q

Cell membrane proteins

A

Ion channels, carriers, receptors, enzymes, linkers, cell identity-markers

49
Q

Cell membrane lipid types

A

Phospholipids, sphingolipids, cholesterol

50
Q

Cell membrane function is dependent on

A

Arrangement/presence of protein and lipids within the bilayer

51
Q

Non-membranous cell inclusions

A

Ribosomes, proteasomes, vaults, protein fibers

52
Q

Rough ER vs. Smooth ER

A

Rough ER: produces proteins
Smooth ER: produce fatty acids, steroids, inactivation/detoxification of drugs

53
Q

Different tissue types have different compositions of organelles/organelle types to accommodate

A

Different functionalities of tissues

54
Q

Mitochondria

A

Site of aerobic synthesis

55
Q

Peroxisomes

A

Contain hydrogen peroxide, serve to detoxify cells, degrade fatty acids

56
Q

Cytoskeleton

A

Cell shape, internal organization, intracellular transport, assembly of cells into tissues, movement

57
Q

Cytoplasmic protein fibers

A

intermediate (keratin, myosin), microtubules (tubulin, flagella, cilia), actin (microfilaments)

58
Q

Smallest –> largest cytoplasmic protein fibers

A

actin, intermediate, microtubules

59
Q

Motor proteins

A

Myosins (muscle contractions), kinesins (movement along microtubules), dyneins (cilia, flagella)

60
Q

Nucleolus function

A

Control RNA synthesis for ribosomes

61
Q

Primary tissue types

A

Epithelial, connective, muscle, nerve

62
Q

CAMs

A

Cell adhesion molecules (include cadherins, integrins, selectins)

63
Q

What proteins facilitate gap junctions?

A

Connexin proteins

64
Q

Gap junctions

A

Create bridges between adjacent cells to allow for VERY fast communication between cells (all cells in a tissue acting together, ex. heart contraction)

65
Q

What proteins facilitate tight junctions?

A

Claudin and occludin proteins

66
Q

Tight junctions

A

Prevent movement between cells

67
Q

Desmosomes

A

Anchor cells to each other

68
Q

What proteins facilitate anchoring junctions?

A

Cadherin proteins

69
Q

Types of cell junctions

A

Anchoring, tight, gap

70
Q

Anchoring junctions

A

Adherens junction, desmosomes, told cells in close contact to either other

71
Q

Composition of epithelial tissues

A

Epithelial cells, basal lamina, underlying tissue

72
Q

Basal lamina

A

Acellular matrix layer secreted by epithelial cells

73
Q

Glandular epithelium

A

Secrete endocrines and exocrines

74
Q

Covering and lining epithelium

A

Forms outer covering of skin (epidermis) and some internal organs, lines lumen of hollow organs (vessels, ducts, digestive, respiratory, urinary, reproductive tracts)

75
Q

Types of connective tissue

A

Loose, dense, adipose, blood, cartilage, bone

76
Q

Connective tissues

A

Most abundant tissues, many types

77
Q

What kind of tissue is blood?

A

Connective tissue

78
Q

What kind of tissue is muscle?

A

Connective tissue

79
Q

Muscle tissue is highly specialized to

A

Contract

80
Q

Three types of muscle

A

Skeletal (striated), cardiac (striated), smooth

81
Q

Nervous tissue

A

Detects and responds to changes in body’s external or internal environment

82
Q

Organs

A

Groups of tissue with related functions (four tissue types in various combinations)

83
Q

Chemical work

A
84
Q

Transport work

A
85
Q

Mechanical work

A

Movement, kinetic and potential energy; utilizing ATP to move muscles to do work

86
Q

Second law of thermodynamics

A

Processes move from state of order to disorder; over time, things break down (entropy) –> you have to overcome entropy to do work

87
Q

Activation energy

A

Energy must be put into the reaction before a reaction can proceed; the push needed to start a reaction

88
Q

Exergonic vs. endergonic energy change

A

Exergonic –> energy released
Endergonic –> energy generated

89
Q

Example exergonic reaction

A

Glucose breakdown (energy released by broken molecule)

90
Q

Endergonic reaction example

A

Synthesizing glucose (energy needed to build molecule)

91
Q

Enzyme function

A

Make activation energy smaller –> more reactions can occur; speeds up reactions without being consumed (help molecules react)

92
Q

Consequence of large activation energy

A

Make reactions irreversible

93
Q

Isozymes

A

Catalyze same reactions but under different conditions –> we all have enzymes that do the same thing but with slight differences individually (polymorphisms, conditional requirements, etc.)

94
Q

Example isozyme

A

Tyrosinase (melanin-producing enzyme), siamese cats have heat sensitive version (will not work in hot spots–> enzyme only active in cool regions of body –> face and tail)

95
Q

Factors that influence rate of enzyme-catalyzed reaction

A

Temp, pH, substrate concentration, non-substrate binding chemicals (inhibitors, modulators), metabolic pathways (feedback inhibition)

96
Q

Protein bonding

A

Disulfide bonds, hydrogen bonds, van der waals forces, ionic bonds/repulsions (all create unique protein shape

Integrative Physiology (13 decks)

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