Biology Flashcards

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1
Q

Thermodynamics vs Kinetics

A

Thermo- spontaneity (Delta G)

Kinetics- rate of rxn (Activation energy, transition state)

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2
Q

Role of catalyst

A

Stabalize transition state

Increase Rxn rate

Decrease activation energy

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3
Q

Enzyme: active site vs allosteric site

A

Active site - substrate binds

Allosteric - different site, can be used for regulation

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4
Q

Competitive inhibition vs non-competitive inhibition

A

Competitive:

  • Compete with s at active site
  • V max is same, Km goes uo

Non Competitive:

  • Bind to allosteric site
  • Lower Vmax (lower binding affinity), Km stays the same
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5
Q

Oxidation vs Reduction

A

Oxidation:

  • Loss of electrons
  • Loss of Hydrogen
  • Gain Oxygen

Reduction:

-Gain e, gain H, lose O

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6
Q

Glycolysis (location/need O?)

A

Cytosol, no

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7
Q

PDC/Krebs (location/need O?)

A

Mit. Matrix, yes indirectly

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8
Q

ETC (location/need O?)

A

Inner mitochondrial membrane, yes directly

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9
Q

Glycolysis Basics

A

6-C (glucose) to 2 3-C (pyruvate)

Net 2 ATP

2 NAD+ -> 2NADH

2 Enzymes: hexokinase (1st step) and phosphorfructokinase 1 (irreversible)

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10
Q

Pyruvate dehydrogenase complex (basics)

A

3 C (pyruvate) to 2 C (acetyl Co-A)

Use: Coenzyme-A

Produce: CO2 and NADH

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11
Q

Krebs/TCA/CAC

A

4-C + 2-C → citrate → 5-C (+CO2) → Oxaloacetate (+CO2 and NADH) → 4-C (+GTP, FADH2, NADH)

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12
Q

E totals (per glucose) from glycolysis, PDC, krebs, and overall

A

Glycolsys (2 ATP and 2 NADH)

PDC (2 NADH)

Krebs (6 NADH, 2 GTP, 2 FADH2)

Net: 30 ATP - euks

32 ATP - proks

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13
Q

Protein synthesis occurs in which direction and with which kind of bond?

A

N to C

Peptide

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14
Q

3 Monosaccharides

A

Fructose, glucose, galactose

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15
Q

3 Dissaccharides

A

Lactose (Glc + Gal)

Sucrose (Glc + F)

Maltose (Glc + G)

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16
Q

3 main polysaccharides

A

Starch, glycogen, cellulose

17
Q

3 Main types of lipids

A

triglycerides, phospholipids, cholesterol

18
Q

amphipathic vs amphoteric

A

pathic - polar and non polar

oteric - acidic and basic

19
Q

DNA: AT vs GC (high melt temp vs low)

A

AT- 2 h-bonds

GC- 3 h-bonds

20
Q

methylation

DNA gyrase

A

Form of DNA protection in prokaryotes only!

Supercoils DNA in proks only!

21
Q

Eurkaryotic DNA structure (histones, nucleosomes, chromatin)

A

Histones + DNA → nuclesomes “beads”

Condensed nucleosomes → chromatin

22
Q

Stop and start codons

A

Start: AUG

Stop: UAA, UGA, UAG

23
Q

Point mutation, missense mutation, nonsense mutation, silent mutation, frameshift mutation

A

Point Mutation: single BP change

  1. missense - different AA
  2. nonsense - early stop codon
  3. silent - diff codon but same AA

Frameshift mutation: insertion or deletion of BP

24
Q

4 Rules of DNA replication

A
  1. Semiconservative
  2. 5’ → 3’
  3. Need primer
  4. Need template
    5.
25
Q

DNA Replication Enzymes: Helicase, primase, dna polymerase, ligase

A

Helicase - unwinds DNA

Primase - Add primer

DNA polymerase - adds bases

Ligase - seals backbone

26
Q

Prokarytoic vs Eukaryotic DNA Replication

A

Prokaryotic:

  1. One origin of rep.
  2. theta rep
  3. 3 DNA Polymerases

Eukaryotic:

  1. Multiple origins
  2. One main DNA Polymerase
27
Q

3 DNA Polymerases

A
  1. Slow, removes primer, 3’ → 5’ and 5’ → 3’ exonuclease
  2. Unknown
  3. fast, edits, proofreads, 3’ → 5’ exonuclease
28
Q

Main differences between replication and transcription

A

Replication has:

  1. stop site
  2. no primer
  3. Lower fidelity!!
29
Q

DNA Transcription: Eukaryotes vs prokaryotes

A

Prokaryotes:

  1. Trxn and trnsln occur same place/time
  2. no mRNA processing
  3. Polycystronic mRNA
  4. One main RNA polymerase
  5. first AA → fMET

Eukaryotes:

  1. trxn in nucleus, transln in cytosol
  2. mRNA processing (5’ cap, poly A tail, splicing)
  3. monocystronic
  4. 3 RNA pol.
  5. first AA is met
30
Q

3 RNA Polymerases

A
  1. rRNA
  2. mRNA
  3. tRNA
31
Q

ribosomes in proks vs euks

A

Proks: 70 s total (30 + 50)

Euks: 80 s total (40 + 60)

(3,5,7)

(4,6,8)

32
Q

E totals for transcription and translation

A

for “n” AA → 4n ATP

ex. 50 AA polypeptide → 199 ATP

33
Q
A