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Integrative Physiology > Lecture 2 > Flashcards

Lecture 2 Flashcards

(96 cards)

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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
Polymer formation
Dehydration synthesis (removal of water to connect peptide chains)
26
Primary protein structure
Sequence of amino acids; influences interactions in secondary sequence
27
Secondary protein structure
Alpha-helix, beta-pleated sheets
28
Quaternary protein structure
Fibrous proteins, globular proteins; contains subunits
29
Protein bonding
Hydrogen bonds, van der waals forces, ionic bonds, ionic repulsions, disulfide bonds --> all generate unique protein structure
30
In order for an enzyme to work, it must be
Soluble
31
How are protein interactions modulated?
Specificity, affinity (proteins are selective about bonding/binding)
32
Isoforms
Functionally similar proteins, encoded by similar genetics but not identical
33
Protein interactions
Binding, selectivity, molecular complementarity (specificity, affinity), isoforms
34
Selective protein binding
Induced-fit model (lock and key mechanism); use of binding sites --> cofactors and inhibitors can alter binding sites/bindings
35
Allosteric activation/inhibition
Changes conformation of protein to allow or inhibit interaction with ligand
36
Influence of pH and temperature on protein
Alter 3D shape of protein by disrupting hydrogen or S-S bonds, may be irreversible if protein denatures
37
Physical factors that affect protein function
Temp, pH, concentration of protein (up and down regulation), concentration of ligands, maximum reaction rate (saturation) --> availability of necessary components
38
Rate of protein activity
Maximal activity at certain temp, pH (optimal range) --> range of rates with varied temps, pH, etc.
39
Nucleotides and Nucleic acids
Comprised of base, sugar, phosphate; transmit and store information (DNA, RNA), transmit and store energy (ATP, cAMP, NAD, FAD)
40
Types of extracellular fluids (2)
Plasma, interstitial fluids
41
Functional compartments of the body
Extracellular (plasma, interstitial fluid) and intracellular fluid
42
Interstitial fluid
Fluid between the circulatory system and cells
43
Difference between extracellular and intracellular fluid
Intracellular - cytoplasm, extracellular - fluid outside cells, fluid in blood
44
Homeostatic difference between extracellular and intracellular fluid
Difference in charge, chemicals, between fluids but differences ARE homeostatic
45
Fluid mosaic model of a membrane
Phospholipid bilayer, membrane contains variety of other proteins, carbohydrates (glycoproteins), cholesterol
46
Cell membrane functions
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
Cell membrane protein types
Integral, peripheral, lipid-anchored
48
Cell membrane proteins
Ion channels, carriers, receptors, enzymes, linkers, cell identity-markers
49
Cell membrane lipid types
Phospholipids, sphingolipids, cholesterol
50
Cell membrane function is dependent on
Arrangement/presence of protein and lipids within the bilayer
51
Non-membranous cell inclusions
Ribosomes, proteasomes, vaults, protein fibers
52
Rough ER vs. Smooth ER
Rough ER: produces proteins Smooth ER: produce fatty acids, steroids, inactivation/detoxification of drugs
53
Different tissue types have different compositions of organelles/organelle types to accommodate
Different functionalities of tissues
54
Mitochondria
Site of aerobic synthesis
55
Peroxisomes
Contain hydrogen peroxide, serve to detoxify cells, degrade fatty acids
56
Cytoskeleton
Cell shape, internal organization, intracellular transport, assembly of cells into tissues, movement
57
Cytoplasmic protein fibers
intermediate (keratin, myosin), microtubules (tubulin, flagella, cilia), actin (microfilaments)
58
Smallest --> largest cytoplasmic protein fibers
actin, intermediate, microtubules
59
Motor proteins
Myosins (muscle contractions), kinesins (movement along microtubules), dyneins (cilia, flagella)
60
Nucleolus function
Control RNA synthesis for ribosomes
61
Primary tissue types
Epithelial, connective, muscle, nerve
62
CAMs
Cell adhesion molecules (include cadherins, integrins, selectins)
63
What proteins facilitate gap junctions?
Connexin proteins
64
Gap junctions
Create bridges between adjacent cells to allow for VERY fast communication between cells (all cells in a tissue acting together, ex. heart contraction)
65
What proteins facilitate tight junctions?
Claudin and occludin proteins
66
Tight junctions
Prevent movement between cells
67
Desmosomes
Anchor cells to each other
68
What proteins facilitate anchoring junctions?
Cadherin proteins
69
Types of cell junctions
Anchoring, tight, gap
70
Anchoring junctions
Adherens junction, desmosomes, told cells in close contact to either other
71
Composition of epithelial tissues
Epithelial cells, basal lamina, underlying tissue
72
Basal lamina
Acellular matrix layer secreted by epithelial cells
73
Glandular epithelium
Secrete endocrines and exocrines
74
Covering and lining epithelium
Forms outer covering of skin (epidermis) and some internal organs, lines lumen of hollow organs (vessels, ducts, digestive, respiratory, urinary, reproductive tracts)
75
Types of connective tissue
Loose, dense, adipose, blood, cartilage, bone
76
Connective tissues
Most abundant tissues, many types
77
What kind of tissue is blood?
Connective tissue
78
What kind of tissue is muscle?
Connective tissue
79
Muscle tissue is highly specialized to
Contract
80
Three types of muscle
Skeletal (striated), cardiac (striated), smooth
81
Nervous tissue
Detects and responds to changes in body's external or internal environment
82
Organs
Groups of tissue with related functions (four tissue types in various combinations)
83
Chemical work
84
Transport work
85
Mechanical work
Movement, kinetic and potential energy; utilizing ATP to move muscles to do work
86
Second law of thermodynamics
Processes move from state of order to disorder; over time, things break down (entropy) --> you have to overcome entropy to do work
87
Activation energy
Energy must be put into the reaction before a reaction can proceed; the push needed to start a reaction
88
Exergonic vs. endergonic energy change
Exergonic --> energy released Endergonic --> energy generated
89
Example exergonic reaction
Glucose breakdown (energy released by broken molecule)
90
Endergonic reaction example
Synthesizing glucose (energy needed to build molecule)
91
Enzyme function
Make activation energy smaller --> more reactions can occur; speeds up reactions without being consumed (help molecules react)
92
Consequence of large activation energy
Make reactions irreversible
93
Isozymes
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
Example isozyme
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
Factors that influence rate of enzyme-catalyzed reaction
Temp, pH, substrate concentration, non-substrate binding chemicals (inhibitors, modulators), metabolic pathways (feedback inhibition)
96
Protein bonding
Disulfide bonds, hydrogen bonds, van der waals forces, ionic bonds/repulsions (all create unique protein shape

Integrative Physiology (13 decks)

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