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Biology 101 > Diversity of Life, Molecules, and Membranes > Flashcards

Diversity of Life, Molecules, and Membranes Flashcards

(61 cards)

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1
Q

Emergent Properties

A

New levels of organization provide new functions.

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2
Q

Order of Organization

A

Domain->Kingdom->Phylum->Class->Order->Family->Genus->Species

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3
Q

Examples of Unity and Diversity

A

Diversity: obvious. Unity: DNA Codes, cilia

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4
Q

Macromolecules

A

Polymers built from monomers

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5
Q

Enzymes; give an example

A

Facilitate reactions. E.g: Sucrase breaking down sucrose

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6
Q

Dehydration and Hydrolysis; which break and which create?

A

Make: Dehydration. Break: Hydrolysis

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7
Q

Glucose Molecular Formula

A

C6H12O6

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8
Q

4 Types of Polysaccharides

A

Starch, Glycogen, Cellulose, Chitin

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9
Q

Starch (Function, Used by)

A

Storage, plants

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10
Q

Glycogen (Function, Shape, Used by)

A

Storage, branched hydrocarbons, animals

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11
Q

Cellulose (Function, Shape, Used by)

A

Structure, long strings, plant walls

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12
Q

Chitin (Function, Used by)

A

Structure, fungi and animal exoskeletons

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13
Q

Fats (Structure; 2 parts)

A

Glycerol and Fatty Acid

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14
Q

Saturated Fatty Acid

A

Saturated Hydrogens, no cis or trans

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15
Q

Unsaturated Fatty Acid

A

Cis or Trans bonding causes kinks that unsaturated the triglycerides.

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16
Q

Good, the Bad, the Ugly(really Bad) (Fatty acids)

A

Unsaturated Fats, Saturated Fats, Trans Fats

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17
Q

Fats: Function

A

Storage, Protection, Insulation

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18
Q

Why are Trans Fats Bad?

A

They increase levels of LDL cholesterol.

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19
Q

Phospholipids(Structure)

A

Hydrophilic head, and Hydrophobic double tail (fatty acids)

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20
Q

Proteins(monomer and polymer)

A

Amino acid monomers, polyPEPTIDE polymers via peptide bonds

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21
Q

Proteins (General use in cell)[1]

A

They are the TOOLS of the cell

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22
Q

Amino acid structure

A

Amino group, R group that provides function, and a carboxylic acid allowing formation of peptide bonds with Amino group

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23
Q

Polypeptides( 2 termini)

A

contains an amino terminus and a carboxy terminus

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24
Q

Proteins (Primary Structure)

A

Polypeptides

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25
Proteins (2 Secondary Structures, and how they are bonded)
Alpha helices and Beta sheets created from hydrogen bonds
26
Proteins (Tertiary Structure causes)[5 interactions]
Interactions between R groups. [Hydrogen bonding, Disulfide bridges, Ionic Bonds, Van Der Waals, and hydro (phobic/philic) exclusions.]
27
Factors that affect enzyme function
Temperature, pH
28
Lipids (3 functions)
Hormones, Energy, Cell membranes
29
Sterols (Steroids)(3 properties, and structure)
Are hormones, largely hydrophobic, used in membrane structure [cholesterol], 4 RING STRUCTURES
30
Lipoprotein Complex
Transport for hydrophobic molecules such as cholesterol. Made of phospholipid ball, apoproteins, and cholesterol.
31
Apo Proteins
Proteins involved in the lipoprotein complex
32
Good and Bad Lipoproteins
Bad: LDL(low density lip...), Good: HDL (high density lip...)
33
LDL and why it's bad in large quantities
carries cholesterol from liver to body cells, can cause plaque buildup
34
HDL
picks up excess cholesterol from cells and delivers back to liver for disposal/recycling
35
Phospholipids (2 structures)
Phospholipid bilayer; micelles
36
4 pieces of a biomembrane
Phospholipid bilayer, proteins, cholesterol, oligosaccharides
37
Function of Cholesterol in Membrane
Gives rigid strength to membrane
38
Oligosaccharides (Where and functions (2))
3-10 monomer polysaccharides attached to membrane proteins and phospholipids. Helps with marker/ID, and connect to cytoskeleton.
39
Factors that affect membrane fluidity(3)
Temperature, phospholipids, steroids
40
How does temperature affect membrane fluidity?
Higher temperature: melting, denaturation | Lower temperature: less fluid/permeable-->solidification
41
What phospholipid characteristics alter membrane fluidity?
Saturated: less fluid/permeable Unsaturated: more fluid/permeable
42
What steroid characteristics alter membrane fluidity?
More cholesterol can increase strength of membrane, but decrease fluidity
43
Glycoprotein
a protein with a carbohydrate attached
44
Types of Transport[General] (2)
Passive Transport and Active Transport
45
Types of Passive Transport (3)
Simple Diffusion, Facilitated Diffusion, Osmosis
46
Simple Diffusion (2 facts)
High to low concentration, movement of small uncharged hydrophobic molecules such as estrogen and testosterone, or GASES
47
Facilitated Diffusion is aided by what kinds of proteins?
Transmembrane channel proteins and Carrier Proteins
48
Channel Proteins (4 facts)
Sometimes gated, requiring a SPECIFIC signal, rapid response, for small molecules
49
Carrier Proteins
Changes shape, for larger molecules, e.g: glucose transporters
50
Osmosis
Movement of water down the gradient, no energy investment
51
Osmosis Channel Proteins are called....
Aquaporins, involved for fast water transfer
52
If the solution a cell is in is HYPERtonic, which way does water move, and what happens to the cell?
If solution is HYPERtonic, water moves from higher concentration IN CELL TO lower concentration OUTSIDE OF CELL. This causes the cell to SHRINK.
53
If the solution a cell is in is HYPOtonic, which way does water move, and what happens to the cell?
If solution is HYPOtonic, water moves from higher concentration OUT OF CELL TO lower concentration INSIDE OF CELL. This causes the cell to BURST.
54
Active Transport (2 facts)
movement against gradient, needs energy
55
Energy process for Active Transport
ATP (Adenisone TRIphosphate) undergoes hydrolysis and loses a phosphate group to mechanism. Comes out as ADP (Adenisone Diphosphate)
56
Active Transport Types (2)
Protein pumps, and Bulk Transport
57
Transmembrane Pumps
Can be very specific proteins that use ATP to change shape, releasing one ion and capturing another into cell.
58
Bulk Transport (Vesicular Transport)(3 types)
Phagocytosis, Pinocytosis, Receptor mediated endocytosis
59
Phagocytosis
LARGE food particles engulfed by membrane
60
Pinocytosis
Bringing in SMALLER RANDOM particle pockets and picking and choosing.
61
Receptor Mediated Endocytosis and example with LDL
Very selective receptors exist on membrane, waiting for specific particles to hit the membrane. E.g : LDL Receptors that bind to apoproteins on LDL lipoprotein complex. Receptors reused.

Biology 101 (12 decks)

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