Biochemistry Ch 1 - AA, Peptides, Proteins Flashcards

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

A

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
Q

Cysteine

A

Side chain has a thiol group = sulfur and hydrogen (-SH)

Can form a disulfide bond if close to another Cystine

26
Q

Disulfide Bridge

A

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
Q

Cysteine vs Cystine

A

e (for electron) lost during disulfide bond formation

It was oxidized (H fell off)

28
Q

Amino Group

A

NH3.
H+ acceptor
Basic.
The Nitrogen is happy making it Pos (+)

pKa ~ 9

29
Q

Carboxylic Acid Group

A

COOH
H+ donor
Acidic
Neg (-) charge

pKa ~ 2

30
Q

pK

A

Negative log of acid dissociation constant

31
Q

Non-polar, Hydrophobic AA

A

H2O Haterz

Alkyl (7) - CH?
Aromatic (2) -

32
Q

Polar, Hydrophilic AA

A

H2O lovers

Contain an O or Sulfur atom

Neutral (6) -
Acidic (2) - have COOH acid
Basic (3) - have N (very positive)

33
Q

Alkyl Group

A

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
Q

Aromatic Group

A

Non polar, hydrophobic

Phenylalanine - benzyl side chain
Tryptophan - lg. Double ring with N

35
Q

Neutral Group

A

Polar, hydrophilic

Have —OH group (amide)

Serine
Threonine
Asparagine
Glutamine
Cysteine -> cystine 
Tyrosine
36
Q

Acidic Group

A

Polar, hydrophilic

Have —COOH- group (carboxylate)

Aspartic Acid -> aspartate
Glutamic Acid -> glutamate

Donate their hydrogen and left in anion form

37
Q

Basic Group

A

Polar, hydrophilic

Have pos charged N atoms

Histidine
Lysine
Arginine

38
Q

Conformational Structure

A

Proper 1°, 2°, 3°, 4° Structures completing the final protein

Active 3D structure

39
Q

Temp Denaturation

A

Breaks the bonds of 2°, 3°, 4°

1° structure ok

40
Q

pH Denaturation

A

Breaks ionic bonds in 3° abs 4°

1° and 2° structures are ok

Like vinegar (H+)

41
Q

Chemical Denaturation

A

Break hydrogen bonds in 2°, 3° and 4°

1° structure ok

42
Q

Enzyme Denaturation

A

All bonds broken in 1°, 2°, 3°, and 4° structures