Biomolecules Flashcards

1
Q

What is the central dogma

A

Theory by Watson and Crick that help explain transfer of sequential info
DNA→RNA→protein

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2
Q

What are the 3 processes involved in converting DNA into proteins

A
  1. replication of DNA
  2. transcription (DNA→RNA)
  3. Translation (RNA→protein)
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3
Q

DNA Replication

A

DNA makes a copy of itself

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4
Q

Transcription

A

DNA converts to RNA

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5
Q

Translation

A

RNA converted into protein

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6
Q

What are 3 violations of the central dogma

A
  1. reverse transcription
  2. RNA viruses
  3. ncRNA
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7
Q

Reverse Transcription

A

When RNA is converted back into DNA resulting in cDNA

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8
Q

Example of Reverse Transcription

A

HIV

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9
Q

RNA Viruses

A

use RNA strand to replicate another RNA strand or the RNA itself just helps out other cells
ex: Corona virus, influenza, measles

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10
Q

Non coding RNA
ncRNA

A

functional molecules that skip translation and RNA just directly helps in cell

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11
Q

Epigenetics

A

study of heritable changes in gene activity that are not caused by changes in DNA sequence
(aka how the environment and other things effect genes)

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12
Q

What holds the primary structure of proteins togehter

A

peptide bonds

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13
Q

What is the main structure of an AA

A
  • alpha carbon
  • amino group
  • carboxyl group
  • side chain
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14
Q

How is a peptide bond formed

A

There is a nucleophilic addition elimination rxn bw the carboxyl and amino group of 2 AA

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15
Q

2 ways to break a peptide bond

A
  1. acid hydrolysis + heat
  2. proteolysis
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16
Q

Hydrolysis

A

use strong acids or proteolytic enzymes to break bonds

16
Q

Acid hydrolysis + heat

A

Non-specific method:
Uses a strong acid and heat to break the peptide bond

16
Q

Proteolysis

A

Specific method:
uses ez protease to break peptide bond

17
Q

What are the 4 Special Case AA

A

Histidine
Proline
Glycine
Cysteine

18
Q

Histidine

A

His, H
pka=6.5
- basic, hydrophilic
- at body pH, can be both protonated and deprotonated
- helps p active site bc it can stabilize/destabilize a substrate

19
Q

Proline

A

Pro, P
- hydrophobic
- secondary alpha amino group
- can disrupt secondary structure of alpha helix by introducing a kink to helix due to secondary alpha amino group

20
Q

Glycine

A

Gly, G
- hydrophobic
- small and flexible (lots of rotation)
- can disrupt secondary structure of alpha helix by introducing a kink in helix due to its flexibility

21
Q

Cysteine

A

Cys, C
- has thiol (SH) group
- prone to make disulfide bonds (most likely to occur in oxidizing environment found extracellularly)
- reduced form of cysteine is common in intracellular space of cell

22
Q

Chiral Carbon

A

has 4 unique groups

23
Q

Chirality

A

optical activity
- when a plain polarized light is on a chiral carbon, then the light will be rotated

24
Q
A