Midterm 1 Flashcards

(55 cards)

1
Q

Prokaryotes

A

no nucleus

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2
Q

Eukaryotes

A

contains DNA containing nucleus

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3
Q

Four Major Families of Biomolecules

A

Sugar, Fatty Acids, Amino Acids, Nucleotides

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4
Q

Monosaccharide

A

simple sugar (CH2O)n with n = 3, 4, 5, 6

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5
Q

Disaccharides

A

two monosaccharides bonded covalently

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6
Q

Oligosaccharides

A

3 to 10 monosaccharide chain

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7
Q

Polysaccharides

A

greater than 10 monosaccharides (10s, 100s, more); can also be called glycans.

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8
Q

Bacterial Growth Phase 1

A

Lag Phase

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9
Q

Bacterial Growth Phase 2

A

Exponential Growth Phase

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10
Q

Bacterial Growth Phase 3

A

Stationary Phase

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11
Q

Bacterial Growth Phase 4

A

Decline Phase

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12
Q

General Equation for Bacterial Growth (exponential)

A

N = Noe^(mut)

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13
Q

General Equation for Bacterial Growth (doubling time)

A

N = No*(2^(t/td))

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14
Q

equation for mu

A

mu = ln2/td

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15
Q

Optimal pH Neutrophiles

A

6-8

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16
Q

Optimal pH Acidophiles

A

<2

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17
Q

Optimal pH Alkaliphiles

A

10

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18
Q

Aerobic

A

Requires O2 for growth/metabolism

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19
Q

Anaerobic

A

Inhibited by presence of O2

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20
Q

Facultative

A

Grow in conditions with or without O2

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21
Q

Heterotrophs

A

use of organic compounds such as carbs, lipids, or hydrocarbons as carbon and energy source.

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22
Q

Autotrophs

A

Use CO2 as a carbon source

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23
Q

Photoautotrophs

A

use CO2 as a carbon source and obtain energy from light

24
Q

Chemoautotrophs

A

use CO2 as carbon source and obtain energy from oxidation of inorganic molecules

25
First Law Thermodynamics
conservation of energy ( in = out )
26
Second Law Thermodynamics
universal increase of entropy
27
Gibbs Free Energy
dG = dH - TdS
28
Anabolic Pathways
large molecules made from smaller ones
29
Catabolic Pathways
large and/or energy containing molecules are broken into smaller ones, releasing energy
30
Activated Carriers
small organic molecules with energy-rich covalent bond(s) or high-energy electrons, easily transferrable
31
Catalysis (protein)
enzymes catalyze intracellular reactions
32
Transport (protein)
control passage of nutrients in/out of cells
33
Structural (proteins)
connective tissues, hair, nails, feathers, horns
34
Molecular Recognition (proteins)
antibodies/immune system
35
Motion (proteins)
cellular transport
36
Primary Structure
amino acid sequence
37
Calculating the number of different shapes a molecule can take
of bond angles ^ number of bonds
38
Hydrophobic effect
The release of water molecules from the structured solvation layer around the molecule as protein folds. Hydrophobic amino acids usually form the “core” of a protein
39
Hydrogen bonds
Interaction of N−H and C=O of the peptide bond leads to local regular structures such as α helices and β sheets.
40
van der Waals
Medium-range weak attraction between all atoms contributes significantly to the stability in the interior of the protein.
41
Electrostatic interactions
- Long-range strong interactions between permanently charged groups – Salt bridges, especially those buried in the hydrophobic core, strongly stabilize the protein.
42
denature
Unfold, but will find its most stable fold after time. the most stable fold is lowest free energy.
43
chaperones
chaperone proteins help other unfolded proteins by trapping them until they are folded properly
44
φ (phi) angle
angle around the α carbon—amide nitrogen bond
45
ψ (psi) angle
angle around the α carbon—carbonyl carbon bond
46
Ramachandran Plot
shows favorable angles
47
Secondary Structure
a local spatial arrangement of the polypeptide backbone.
48
alpha helix
- stabilized by hydrogen bonds between nearby residues - right handed helix
49
beta sheet
- formed from H-Bonding of amines. - the planarity of the peptide bond and tetrahedral geometry of the α carbon can create a β strand.
50
random coil
irregular arrangement of polypeptide chain
51
strong helix breaker
pro, gly
52
strong helix formers
ala, leu
53
two types of beta sheets
parallel: -----> -----> -----> antiparallel: -----> <----- ----->
54
Amyloid
- beta sheets stacked together into long strands - can result from protein misfolding - associated with neurodegenerative diseases
55