Concept 1: Biomolecules Flashcards

1
Q

Isoelectric point

A

the average pKa’s of the groups in the amino acid

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2
Q

The pKa of COOH and NH3+

A

2 and 9-10

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3
Q

Primary structure of a protein consists of:

A

Peptide bonds

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4
Q

Secondary structure of a protein consists of:

A

backbone interactions, H-bonds, a-helices, and B-sheets

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5
Q

Tertiary structure of proteins consists of:

A

H-bonds, salt bridges, van der waals, hydrophobic interactions, S-S (heavy metal is a reducing agent).

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6
Q

If you add alcohol to a protein, what happens?

A

disrupts secondary, tertiary bonds and H-bonds

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7
Q

Temperature to a protein does what?

A

denatures to the primary structure

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8
Q

pH does what to protein?

A

breaks down until the secondary structure and salt bridges

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9
Q

What are the four types of enzymatic functions?

A
  1. acids/base (protons) 2. covalent catalysis (electrons) 3. Electrostatic 4. Proximity and orientation
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10
Q

delta G with double dagger means:

A

free energy of activation (Ea)

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11
Q

delta G with degree means:

A

standard free energy of change (Erxn)

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12
Q

What are the 6 types of enzymes (not functions)

A
  1. Transferase-move functional groups 2. Ligase-break bonds with ATP 3. Oxidoreductase 4. Isomerase 5. Hydrolase (Protease) 6. Lyase-make double bond or ring to cleave
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13
Q

Cofactors are:

A

nonorganic, directly involved in reaction (e.g. Mg2+)

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14
Q

Coenzymes are:

A

organic carriers (e.g. NADH)

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15
Q

Ester functional group

A

C-CO-O-

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16
Q

Anhydride functional group

A

-CO-CO-

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17
Q

Michaelis-Menton Constant

A

In terms of Molarity and think of it as affinity. Dissociation over association. KM=[S] to achieve 1/2 Vmax.

18
Q

Michaelis-Menton Equation

19
Q

What is Kcat?

A

Catalytic Turnover (s-1): Kcat=Vmax/[E]T

20
Q

What is catalytic efficiency?

A

KA=Kcat/KM Bigger the number, the better.

21
Q

Lineweaver Burke Plot

A

Inverse of Michaelis-Menton Equation.

22
Q

Lineweaver Burke Equation

23
Q

Competitive Inhibitor

A

Binds to free enzyme. This changes the slope (KM/Vmax) but not the Y-int (Vmax). You can add [S] to overcome Inhibitor.

24
Q

Uncompetitive Inhibitor

A

Binds to bound enzyme. Can enhance E+S binding. No change in slope (KM/Vmax) and a change in Y-int (1/Vmax). KM and Vmax change proportionally.

25
Noncompetitive Inhibitor
Also known as mixed inhibitor. Binds to free and bound enzymes. Increase slope (KM/Vmax) and Y-int (1/Vmax).
26
Homotropic regulator
A molecule that is a substrate and a regulator in a feedback loop
27
Heterotropic feedback loop
The substrate and the regulator molecule are different
28
What are the covalent modifications?
1. Post-translational modifications (ER/golgi: glycosylation, lipidation, ubiquination (destruction) and phosphorylation) 2. Co-translational modification (acetylation) 3. Zymogen (inactive form) 4. "Suicide" (permenant inactivation)
29
Base + Deoxyribose =
Nucleoside
30
What nucleotides are purines?
Pure As Gold: Adenine and Guanine
31
What nucleotides are pyrimidines?
Thymine and Cytosine
32
Phosphate + nucleoside =
Nucleotide
33
What polarity (way) does DNA replication run?
5'--\>3'
34
What way do nucleotides link?
3'--\>5'
35
The phases of transcription and where it happens
Happens in the nucleus. Initiation, elongation, and termination. The coding strand is identical to the sequence, however, the template strand, which is complementary, is read.
36
Translation
Occurs in the cytoplasm in ribosomes. APE sites.
37
Mismatch repair system
remove by enxonuclease usually during DNA synthesis.
38
Nucleotide Excision Repair
Removal of bumps (helical distortion) by removing the whole incorrect strand and adding new ones. Good for UV damage--pyrimidine dimers.
39
Base excision repair
Removal of bases that usually do not cause distortion in helical shape.
40
DNA Hybridization
The annealing of DNA pairs by A-T and C-G of complementary strands.
41
DNA Annealing
When base complements bind by hydrogen bonding. Usually to describe a primer binding to a DNA sequence during PCR reaction.