L.3 Biopolymers: DNA, RNA, Proteins Flashcards

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1
Q

L.O.

A
  • Identify the conventions of direction/ends of protein and nucleic acids.
  • Describe the repeating units (backbones and sidechains or bases) in proteins and nucleic acids
  • Identify the main chemical components of nucleic acids and proteins/peptides.
  • Describe how the physical and chemical properties of proteins and nucleic acids can be exploited in experimental situations.
  • Appreciate that DNA is the source of genetic information
  • Describe the base pairing between nucleobases and appreciate that C/G base pairing is stronger than A/T(U) base pairing in nucleic acids
  • Describe the double-helical structure of DNA
  • Distinguish DNA from RNA in terms of structure and stability
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2
Q

Biopolymers

A
  • Info containing
  • Have a defined beggining and end
  • Synthesized in 1 direction only, increasing the backbone
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3
Q

Nucleic acids

A

5’ to 3’

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4
Q

Proteins

A

N’ to C’ (N terminus to C terminus)
- N from Nitrogen in Amino terminus, C from carbon in Carboxy terminus

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5
Q

Residues (terminology)

A

Refers to a single amino acid on a protein chain
- Eg, ‘T’ in ‘ATYHWLLLGAD’

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6
Q

Nucleic acid polymers

A

DNA / RNA
- Build from phosphate, sugar, base/ nucleobase
- 5’ to 3’

[heft]

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7
Q

DNA Vs RNA bases

A

DNA:
- Adenine = T
- Guanine = C
- Cytosine = G
- Thymine = A

RNA:
- Adenine = U
- Guanine = C
- Cytosine = G
- Uracil = T

Apple = Tree
Car = Garage

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8
Q

Properties of the common backbone

A
  • Common, no matter the base
  • -ve charge (Phosphate)
  • Hydrophilic (Sugars & phosphate)
  • Makes it well suited to electrophoresis
  • Ethanol precipitation
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9
Q

Proteins

A
  • Amino acid = monomer
  • Common peptide backbone ( N-C-C)
  • 20 different amino acid side chains

[heft]

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10
Q

Peptide bond formation

A
  • 2 amino acids combine via condensation reactions to form a dipeptide
  • Uses lots of energy

[heft]

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11
Q

Peptide bond resonance

A
  • e- are rearranged upon creation of peptide bonds (can be shared to create equilibrium and fullfiull octet rule)
  • Leaves an overall partiual charege on LHS & RHS
  • Makes the backbone polar, encouraging hydrogen bonding
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12
Q

Peptide backbone

A

[heft]

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13
Q

Amino acid side chains

A

[heft]

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14
Q

Aromatic protein sidechains and nucleobases

A
  • There are 3 aromatic amino acid sidechains

Aromatic sidechains absorb light at:
- Protein ~280nm
- Bases ~260nm

  • Aromatic rings are flat/ planar
  • Absorbtion shows a molecule may be pure / contains DNA/ RNA
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15
Q

Base Pairing

A
  • 2 strands (each helix) are bonded together at complementary bases by hydrogen bonds
  • C & G bonds are stronger
  • A & T = 2x H bonds
  • C & G = 3x H bonds

[heft]

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16
Q

DNA Double Helix: B-DNA

A
  • Strands run in opposite directions
  • Bases are aromatic and flat, stack on eachother
  • -ve charged phosphates repel eachother
  • B-DNA is A symetric with major & minor grooves

[heft]

17
Q

RNA

A
  • Does NOT form B-type structure
  • The extra OH group on the sugar stops it forming long B-DNA helices, making RNA much more sesceptible to degradation
18
Q

DNA Vs RNA

A
  • Bases are very stable generally, except fot sponaneous deamination of C to U. (loses NH3 group from cytosine, turning into uracil)
  • If deamination occurs in DNA, it is converted back into Cytosine quickly.
  • If occurs in RNA, does not repair