1.1 Biomolecule basics Flashcards

1
Q

Which stereochemical configuration is predominant in nature?

A

R stereochemistry / L configuration

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2
Q

Is glycine a chiral molecule?

A

No, achiral, two same side chains (H) at alpha C

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3
Q

What are the amino acid types?

A
  1. Hydrophobic
  2. Acids
  3. Amides
  4. Bases
  5. Aromatics
  6. Alcohols
  7. Thiol / tiolether
    Selenocysteine (21st)
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4
Q

Explain peptide bond formation

A
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5
Q

What are Φ (phi) and Ψ (psi) bonds in a peptide? How are they different from the peptide bond?

A

Φ (phi) and Ψ (psi) bonds are free to rotate because they are stabilised by free e pair of N - π bond can be created

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6
Q

What strcutures are formed in secondary protein structure? Which atoms interact to form what bonds?

A

Repeated α-helices and β-sheets are formed by H-bonds between backbone atoms

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7
Q

How are α-helices formed?

A
  • COOH is H-bond acceptor
  • N is H-bond donor
  • forms between n and n+4
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8
Q

Why is proline known as helix breaker?

A

Cyclic side chain of proline has no N to donate H-bond

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9
Q

How are β-sheets formed?

A
  • COOH is H-bond acceptor
  • N is H-bond donor
  • forms between antiparallel β-pleats to form β-sheet (can form parallel - less stable)
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10
Q

How are tertiary protein structures formed?

A

By side chain interactions of DOMAINS:
- hydrophilic - hydrophobic
- H-bonds
- covalent (disulphide bridge)
- ionic inter.
- electrostatic inter.

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11
Q

How are quaternary protein structures formed?

A

By side chain interactions of SUBUNITS:
- hydrophilic - hydrophobic
- H-bonds
- covalent (disulphide bridge)
- ionic inter.

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12
Q

What are the structures of quarternary proteins? What are their characteristics?

A
  • Globular
  • Fibrous
  • Molecular machines (ATP synthase)
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13
Q

What is the function of protein post-translational modifications (PTMs)?

A

PMTs are covalent processings that change the properties of a protein - makes them functional

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14
Q

What are heteroproteins?

A

Proteins which have non am. a. components (prosthetic groups) ex: nucleotides / redox active groups

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15
Q

Explain the structure of a nucleotide?

A
  • Phosphate (at 5C)
  • Nitrogenous base (at 1C)
  • Ribose (2 OH) / deoxyribose (1 OH) sugar
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16
Q

What kind of nitrogenous bases are there?

A

PURINES: guanine and adenine [GrynAi]
PYRAMIDINES: cytosine, thymine, uracil

17
Q

Why is RNA less stable than DNA?

A

RNA is susceptible to RNA hydrolysis because of extra OH group - RNA more functionally involved, so no need to persist - DNA for long term storage

18
Q

How do nucleotides bond between each other?

19
Q

How do complementary nucleotides bond?

20
Q

Why do thermophilic bacteria have more C-G repeats than A-T?

A

Because C-G form 3 H-bonds while A-T 2 - more stable DNA

21
Q

Which direction is DNA synthesised?

A

5’ -> 3’ end

22
Q

Why is DNA acidic?

A

DNA is acidic because negative charge on phosphate can be protonated / deprotonated

23
Q

What effect additionally stabilises DNA?

A

Intrastrand π stacking between aromatic ring π e stabilises DNA (Van der Waal’s interactions)

24
Q

What forms of DNA are there?

A
  • A DNA
  • B DNA (most common)
  • Z DNA
25
How are nucleotides added in DNA replication?
dNTPs are added (extra 2 phosphates) - pyrophosphate kicked out
26
Why are there more DNA / RNA codons than possible am. a.?
64 codons for 20 am. a. - several codons code for same proteins - to minimise mutation effects
27
Why do bacterial 50S and 30S ribosome subunits add up to 70S ribosome?
its total is not 80s because sedimentation rate (how quickly parts settle in a test tube after centrifugation) of a particular ribosome is not equal to the total of 50s and 30s subunits.
28
What are the ribosomal sites and their functions?
- Site A: tRNA with next am. a. bound - Site P: tRNA with polypeptide chain bound - Site E: am. a. empty tRNA exits
29
What is the mechanism of peptide bond formation in ribosomes?
30
What are the main types of lipids? What are their main characteristics?
1. Fats / oils (saturated / unstaturated fatty acids) 2. Phospholipids (polar - non-polar parts) 3. Steroids (polycyclic molecules) 4. Waxes (extremely hydrophobic)
31
Compare fats vs oils
FATS: - solid at room T - saturated - single bonds (sp3 C - rotation possible) - maximise Van der Waal's - packing more efficient - higher melting point OILS: - liquid at room T - unsaturated - double bonds (sp2 C - no rotation) - kinks - less efficient packing - lower melting point
32
Explain the structure of a triglyceride and its formation
33
Explain the structure of a phospholipid