Biochemistry Ch 1 - AA, Peptides, Proteins Flashcards

(42 cards)

1
Q

Central Dogma

A

DNA -> RNA -> Protein

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2
Q

Replication

A

DNA copies itself

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3
Q

Transcription

A

DNA copied into RNA

Script for using nucleic acids

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4
Q

Translation

A

RNA translated into protein

Translating nucleic acids into amino acids

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5
Q

Reverse Transcription

A

Reverse Transcriptase makes RNA into complementary cDNA

Retroviruses (HIV)

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6
Q

ncRNA

A

Noncoding RNA, function as tRNA or rRNA within the cell

Skips the last step of translation into protein

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7
Q

Epigenetics

A

Changes of gene activity

DNA sequence modified resulting in different phenotype but original DNA sequence stays the same

All DNA the same in different cells (muscle vs epithelial) yet they don’t look or act the same

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8
Q

Amino Acid Structure

A
Carboxyl acid group (HOOC)
Amino group (NH3)
H atom 
R group - different in every AA
Alpha carbon - center
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9
Q

Enantiomers

A

Pair of AA that have mirror image of each other.

L-aa (left amino group) (the ones made in humans)
D-aa (right amino group)

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10
Q

Isoelectric point of AA (pI)

A

Iso=equal. Neither pos or neg charge

Net charges change when H ions are added or removed. Changing pH

Low pH = inc H+ = amine +1 charge (POS AA)

High path = inc OH- = carb group -1 charge (NEG AA)

(pKa1 (amino) + pKa2 (carb)) / 2 = pI

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11
Q

Zwitterion

A

Hybrid

AA that has a net zero charge

Because NH3 is (+) and COOH is (-) charged

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12
Q

Peptide bond

A

Connects 2 AAs

COOH looses OH and NH2 looses H creating H2O

N=C

Double bond so can’t move

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13
Q

α - helix (secondary structure)

A

AA helix where C=O group form a hydrogen bond with N-H group 4 AAs does the spiral.

R groups just stick out

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14
Q

β - pleated sheet (secondary structure)

A

Antiparallel sheet: AA starts with Carboxyl group and the second AA below starts with Amino group
Symmetrical hydrogen bonds: 1AA + 1 AA

Parallel sheet: both AA start with Carboxyl group.
Unsymmetrical hydrogen bonds: 1 AA binds with 2 AA

N-H + O=C

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15
Q

Tertiary structure

A

Secondary structures coming together where AA side chains interact with each other

H bonds, ionic bonds, disulfide bonds

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16
Q

Hydrolysis

A

Breaking the peptide bond

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17
Q

Acid Hydrolysis

A

Strong acid + heat to break peptide bond

18
Q

Proteolysis

A

Protease breaks the peptide bond

Specific - choose which AA to break

19
Q

Trypsin

A

Protease that breaks carboxyl side like Arginine or Lysine

Produced by pancreas to digest food

20
Q

Histidine

A

-pKa 6.5 which is close to physiological pH 7.4

Can exist as protonated (+) and deprotonated (-) forms

Can stabilize and destabilize a substrate

21
Q

Protonated

22
Q

Deprotonated

A

pH > pKa of AA = negative charge

23
Q

Proline

A

Has a secondary alpha amino group

The side chain forms a second bond with the alpha Nitrogen

Alpha helix breaker = adds a kink to the α helix

24
Q

Glycine

A

Side chain is just one H atom

No chiral carbon = optical activity under polarized light

Very flexible

Alpha helix breaker = adds a kink to the α helix

25
Cysteine
Side chain has a thiol group = sulfur and hydrogen (-SH) Can form a disulfide bond if close to another Cystine
26
Disulfide Bridge
Redox reaction: OIL RIG Oxidation is Loss Reduction is Gain When 2 Cystines are next to each other they are in reducing form (have 2 extra H) 2 H float away (oxidation) creating a bond between the Sulfides in the EXTRACELLULAR space
27
Cysteine vs Cystine
e (for electron) lost during disulfide bond formation It was oxidized (H fell off)
28
Amino Group
NH3. H+ acceptor Basic. The Nitrogen is happy making it Pos (+) pKa ~ 9
29
Carboxylic Acid Group
COOH H+ donor Acidic Neg (-) charge pKa ~ 2
30
pK
Negative log of acid dissociation constant
31
Non-polar, Hydrophobic AA
H2O Haterz Alkyl (7) - CH? Aromatic (2) -
32
Polar, Hydrophilic AA
H2O lovers Contain an O or Sulfur atom Neutral (6) - Acidic (2) - have COOH acid Basic (3) - have N (very positive)
33
Alkyl Group
Non polar, hydrophobic Contain 1 to 4 carbons Glycine - has only H for the R group Alanine - Methionine - has but methyl makes it nonpolar Isoleucine - Valine - Leucine - Proline-cyclic. Connects to amino group from α-Carbonsbbmn
34
Aromatic Group
Non polar, hydrophobic Phenylalanine - benzyl side chain Tryptophan - lg. Double ring with N
35
Neutral Group
Polar, hydrophilic Have —OH group (amide) ``` Serine Threonine Asparagine Glutamine Cysteine -> cystine Tyrosine ```
36
Acidic Group
Polar, hydrophilic Have —COOH- group (carboxylate) Aspartic Acid -> aspartate Glutamic Acid -> glutamate Donate their hydrogen and left in anion form
37
Basic Group
Polar, hydrophilic Have pos charged N atoms Histidine Lysine Arginine
38
Conformational Structure
Proper 1°, 2°, 3°, 4° Structures completing the final protein Active 3D structure
39
Temp Denaturation
Breaks the bonds of 2°, 3°, 4° 1° structure ok
40
pH Denaturation
Breaks ionic bonds in 3° abs 4° 1° and 2° structures are ok Like vinegar (H+)
41
Chemical Denaturation
Break hydrogen bonds in 2°, 3° and 4° 1° structure ok
42
Enzyme Denaturation
All bonds broken in 1°, 2°, 3°, and 4° structures