Amino Acid 1 & 2 Flashcards

1
Q

What is protein structure?

A

The functional properties of most proteins depend upon their 3D structure. The 3D structure is dependent on the sequence of the protein.

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2
Q

What is the primary structure?

A

The sequence

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3
Q

What is secondary structure?

A

Localised pieces of regular structure

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4
Q

What is tertiary structure?

A

The packing of secondary structural elements into one or more globular units (domains).

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5
Q

What is quaternary structure?

A

The interactions of several independent polypeptides to form the final overall protein structure.

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6
Q

How most amino acid is encoded?

A

L- isomer, it has S absolute configuration.

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7
Q

What are L and D?

A

L and D derived from optical properties of glyceraldehyde in solution. The polarised light is rotated by a molecule.
CORN rules.

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8
Q

What are S and D?

A

R and S are absolute configurations of atoms.

R= clockwise, S= anti-clockwise

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9
Q

What is the difference between protein and RNA/DNA?

A

The sequences in proteins are different from sequence in RNA and DNA. RNA and DNA are just symboled to get to protein.

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10
Q

What is peptide bond and how does it work?

A

The peptide bond is the bond linking both amino acid together. The peptide bond is formed by a condensation reaction between amino acid.

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11
Q

What configuration is in the folded proteins?

A

Trans configuration, because it is more energetically favourable than cis. 180º trans

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12
Q

Why proline is in cis configurations?

A

Only proline is in cis configurations because in either trans and cis will have clashing. 0º cis

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13
Q

What is peptide bond also called?

A

Omega bond

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14
Q

What is φ Phi bond?

A
  • Torsional angle around the Cå-N bond.
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15
Q

What is ψ Psi bond?

A

Torsional angle around Cå-C bond.

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16
Q

What is Ramachandran Plot?

A

Graph shows ψ and φ allowed or disallowed in protein structures.

17
Q

Alpha Helix characteristic

A
  • Rotation around helix = 100º per residue
  • 3.6 residue each complete turn
  • First residue hydrogen bond t the fifth residue (Ri-Ri+4)
  • NH point in the same direction
  • Right-handed helix and energetically more favourable, the smaller steric clash between side chain and main chain.
  • Ferritin, iron storage protein
18
Q

Helix dipole characteristics

A

N-terminal (+ve)

C-terminal (-ve)

19
Q

Beta strand

A

R group point opposite direction

20
Q

Parallel Beta strand

A
  • trapezoid shape between strand

- N terminus —-> C terminus for all strand

21
Q

Anti-parallel Beta strand

A
  • Square shape between strand

C terminus C terminus

22
Q

Beta turns

A

First residue hydrogen-bonded to the fourth residue

- Ri- Ri+3