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Bio Final SI stuff > Part 1 > Flashcards

Part 1 Flashcards

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1
Q

Darwin’s observations/Conclusions

A
  1. Organisms evolve to suit their environment
  2. Individuals in a population vary in heritable traits
  3. Competition happens when there’s more offspring than capable of surviving and reproducing
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1
Q

What makes H bonding special?

A

Partial charges due to difference in electronegativity

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2
Q

What is the top number in the wonky periodic diagram?

A

Number of protons and neutrons

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3
Q

What is the bottom number in the wonky periodic diagram?

A

THe number of protons

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4
Q

What are the emergent properties of H2O?

A
  1. Cohesion (due to IM forces)
  2. Moderate temp (High specific heat)
  3. Expansion, ice < dense than H2O (when freezing, due to H bonding)
  4. Universal solvent (Polar, dissolves other things easily, creating hydration shells)
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5
Q

Ph increases, H+ concentration

A

decreases

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6
Q

Why is Carbon the building block of life?

A

forms a lot of bonds, and can bind to all organic elements we need

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7
Q

What are the three types of isomers?

A

Enantiomers- Mirror
Cis-trans- Different spatial arrangement
Structural- Bonding patterns differ

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8
Q

Why are hydroxyl groups important?

A

Polar covalent, can interact with H2O or other polar molecules

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9
Q

Why are carbonyl groups important?

A

Part of ketones and aldehydes

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10
Q

Why are carboxyl groups important?

A

Act as acids, can raise H+ ion concentration in solutions, important for Amino acids

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11
Q

Why are amino groups important?

A

Act as bases, can lower H+ ion concentration in solution, important for AAs.

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12
Q

Why are sulfhydryl groups important?

A

In cysteine (Amino acid), help make 2ndary protein structure

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13
Q

Why are phosphate groups important?

A

High electronegativity of Oxygen’s gives negative charge- can react with water found in ATP

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14
Q

Why are methyl groups important?

A

Decrease transcription by regulating gene expression and changing shape and function of sex hormones

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15
Q

Polymer of lipids

A

None

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16
Q

Polymer of nucleic acids

A

Nucleic acids

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17
Q

Carbohydrate bonds

A

Glycosidic linkages

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18
Q

Protein bonds

A

Peptide bonds

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19
Q

Lipid bonds

A

Ester linkages

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20
Q

Nucleic acid bonds

A

Phosphodiester bonds

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21
Q

What is the main monosaccharide of carbohydrates?

A

Glucose

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22
Q

What are the types of proteins?

A

Enzymatic, digestive, motor, contractile, defense, transport, receptor

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23
Q

What are some types of lipids?

A

Fats, phospholipids, steroids

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24
What is the purpose of carbohydrates?
Short term energy, building materials,
25
Purpose of proteins
Basically everything
26
Purpose of nucleic acids
Storing genetic info
27
Secondary protein structure
Coiling/folding due to H bonds between common components (Alpha helix, beta sheet)
28
Teritary structure of proteins
R group/side chain interactions
29
Quaternary structure of proteins
Multiple polypeptides interacting
30
What is a difference between prokaryotic and eukaryotic cells?
Eukaryotic have membrane bound organelles
31
What does the nucleus do?
hold dna/rna
32
What does the golgi body do?
Saends and packages things outside the cell
33
What do ribosomes do?
Make protein
34
What does the smooth ER do?
Make lipids
35
What does the rough ER do?
Makes membrane
36
What distinguishes smooth and rough ER?
RibosomesW
37
What do lysosomes do?
Digest things
38
What do peroxisomes do?
Perform oxidation
39
What aer the three fibers that make up the cytoskeleton?
Microtubules, microfilaments, intermediate filaments
40
What do microtubules do? What are they made of?
Move chromosomes, tubulin
41
What are microfilaments made of? What do they do?
Actin and myosin, help muscles contract
42
What do intermediate filaments do?
Anchor nucleus/organelles
43
What do desmosomes do?
Fasten cells into strong sheets
44
What do tight cell junctions do?
Prevent ECF fluid leakage
45
What do gap cell junctions do?
Make cytoplasmic channels for cell-cell communication
46
What do plasmodesmata do?
Connect plant cells
47
What is the purpose of the plasma membrane?
Let certain things in and out
48
What is the structure of the plasma membrane?
Phospholipid bilayer with hydrophobic heads and hydrophilic tails
49
What other lipid do we find in the plasma membrane? What does it do?
Cholesterol, regulates membrane fluidity at different temperature
50
What are membrane proteins? What do they do?
Proteins spanning with of membrane that let certain things in and out that can't go by themselves
51
Carrier proteins
Shape change (find ex and add more detail)
52
Channel proteins
TunnelPe
53
Peripheral proteins
Surface of cell
54
Integral proteins
Span into plasma membrane interior
55
Transmembrane proteins- Subtype of what?
Span entire membrane (special type of integral protein)
56
What does the sodium potassium pump do? Why?
Regulates Na/K levels, lets in 2 K and 3 Na out. Maintains negative internal charge through net loss of cations
57
Diffusion- type of transport and concentration
Passive transport, high to low concentration
58
Osmosis, (What it transports and in what direction)
H2O diffusion, low to high solute concentration
59
Do cells gain or lose water in hypertonic solutions?
Lose
60
Do cells gain or lose water in hypotonic solutions?
Gain
61
Does active transport move with or against concentration gradient?
Against
62
Does passive transport move with or against concentration gradient?
With
63
What's the difference between simple and facilitarted diffusino
Facilitated requires help of transport proteins (still doesn't need energy) but simple doesn't
64
Exergonic reactions
Release energy
65
Endergonic rxns
Require energy
66
Do enzymes change Gibb's free energy of a chemical reaction?
No
67
What is Gibb's free energy?
Enthalpy+temp+entropy
68
What is the structure of ATP?
Adenine attached to 3 phosphates and ribose sugar
69
How is ATP broken down? What happens there? What type of reaction does this usually form?
Breaking last phosphate group, usually phosphorylates another molecule, powering an endergonic rxn
70
What are cofactors? What are some examples?
Non protein helpers that facilitate a reaxtion by binding to an enzyme with a substate, eg inorganic metal ions like zinc, iron, copper
71
What are coenzymes?
Organic cofactors (eg most vitamins)
72
What are competitive inhibitors?
Bind to active site, blocking other things from bonding
73
What are noncompetitive inhibitors
Bind to allosteric site, changing shape of actice site

Bio Final SI stuff (2 decks)

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