Primary Structure Flashcards

(27 cards)

1
Q

Who and what year was the protein structure divided into 4 levels?

A

1951 Linderstrøm-Land

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2
Q

What is the primary structure of a protein?

A

It is the sequence of amino acids joined together by peptide bonds

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3
Q

How many amino acids from which almost all proteins are composed of?

A

20 alpha-amino acids

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4
Q

How are proteins which contain amino acids outside the usual 20 amino acids produced?

A

Post translational chemical modification

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5
Q

What is a alpha amino acid composed of?

A

Amine group NH2
Carboxyl group COOH

Both attached to the same carbon center

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6
Q

What does enantiomorphs mean?

A

mirror images exist of the proteins

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7
Q

Where is the L(S) form found?

A

In naturally forming proteins

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8
Q

How do amino acids differ from one another?

A

By its R-Sidechain

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9
Q

If R is a hydrogen atom, what is the amino acid?

A

glycine

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10
Q

If R is a methyl group (CH3), what is the amino acid?

A

Alanine

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11
Q

What within the amino acids determines its three dimensional structure?

A

The physical and chemical properties of the sidechains in a amino acid

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12
Q

What parameters are used to characterize amino acids?

A

Charge
Polarity
Hydrophobicity
Aromaticity
Size

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13
Q

Describe the charge in relation to amino acid classification.

A

Formation of salt bridges or ion pairs

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14
Q

Describe the polarity in relation to amino acid classification.

A

Formation of hydrogen bonds

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15
Q

Describe the hydrophobicity in relation to amino acid classification.

A

Hydrophobic amino acids stabilize the protein core.

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16
Q

Describe the aromaticity in relation to amino acid classification.

A

Interaction with amide or amino groups

17
Q

Describe the size in relation to amino acid classification.

A

important for the packing within the protein, complementarity of the van der Waals surfaces

18
Q

What are peptides?

A

Two or more amino acids joined together by peptide bonds

19
Q

How is a peptide bond formed?

A

A peptide bond is formed when the a-carboxyl of one amino acid is joined to the a-amino of a second amino acid (with the removal of water)
Only a-carboxyl and a-amino groups are used , not R-group carboxyl or amino groups

20
Q

What is Phi?

A

The angle around N-Ca(alpha)

21
Q

What is Psi?

A

The angle around Ca-C’

22
Q

What is a Ramachandran plot?

A

It is a way to visualize backbone dihedral angles Phi against Psi of amino acid residues in the protein structure.

23
Q

Who invented Ramachandran plots and when?

A

G.N Ramachandran
1963

24
Q

What does the white areas correspond to in the plot?

A

correspond to conformations where atoms in the polypeptide come closer than the sum of their van der Waals radii.
The regions are sterically disallowed for all amino acids.

25
What amino acid is sterically allowed in the white region? (What is the exception of the amino acid in the white area?)
Glycine, it is unique as it lacks a side chain
26
What do the red regions correspond to?
Correspond to conformations where there are no steric clashes I.e these are the allowed regions namely the a-helical and b-sheet conformations
27
What do the yellow areas show?
Show the allowed regions if slightly shorter van der Waals radii are used in the calculation. I.e the atoms are allowed to come a little closer together which brings out an additional region which corresponds to the left-handed a-helix