Proteins structure Flashcards

1
Q

What is the primary structure of a protein

A

the linear amino acid sequence of the polypeptide chain

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2
Q

What is the secondary structure of a protein
How is it stabilised

A

the local spatial arrangement of polypeptide backbone – the conformations like helices etc
stabilised by intramolecular and sometimes intermolecular hydrogen bonding of amide groups.

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3
Q

What is the tertiary structure of a protein

A

the overall 3- dimensional configuration of the protein in space

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4
Q

What is the Quaternary Structure of a protein?

How is it held together?

A

association between different polypeptides to form a multi-subunit protein
Each of the subunits has its own primary, secondary, and tertiary structure. The subunits are held together by hydrogen bonds and van der Waals forces between nonpolar side chains.

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5
Q

How is a peptide bond formed

A

Peptide bond formation:
the linking of two amino acids is accompanied by the abstraction of a molecule of water
It occurs between the COO and the NH3
This reaction is also known as a condensation reaction

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6
Q

What are the features of peptide bonds

A
  • Peptide bonds are planar (Straight line)
  • Peptide bonds are rigid
  • Peptide bonds always adopt a Trans Configuration
  • Bonds on either side of the peptide bond are free to rotate
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7
Q

-Why is a peptide bond planar
-What does it mean when planar

A
  • planar bond because it has a partial double bond character.
  • Ca, C, O, N, H and Ca all lie in the same plane
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8
Q

Why is the peptide bond RIGID

A
  • because it has a partial double bond character between
    C-N and C-O
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9
Q

Why is a Peptide bond always adopting a trans confirmation

A

The peptide bond nearly always has the trans configuration since it is more favourable than cis
the reason for this is that the cis isomer places the R groups of the two connected amino acids in close proximity to each other thus they may react with each other in cis

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10
Q

What does the amino acid sequence determine

A

The amino acid sequence of a protein determines:
* The way in which the polypeptide chain folds
* The physical characteristics of the protein

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11
Q

What are the key properties of proteins

A
  1. Size
    * Number of amino acid residues
    * Molecular weight in kDa - (weight of one H Atom)
  2. Isoelectric point
    * The isoelectric point, pI, of a protein is the pH at which there is no overall net charge
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12
Q

What stabilises the Alpha Helix

A

H-bonds between N-H and C=O stabilise the structure of the a-helix

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13
Q

How many amino acids are in one turn of an alpha helix structure?

A

3.6 amino acids

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14
Q

what is a pitch and how long is it in a alpha helix

A

The Distance of one turn
0.54 nm

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15
Q

What helix is alpha helix

A

Right handed helix

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16
Q

What is the distance between two Amino Acids in an alpha helix

A

0.15 nm

17
Q

What is the distance between two Amino Acids in a beta-sheet

A

0.35 nm

18
Q

How is the beta-helix stabilised

A

The structure is stabilised by H-bonds between strand

19
Q

What are the two types of Tertiary Structures

A

Globular proteins:
* Compact structure
* Usually several types of secondary structure
Fibrous proteins:
* Extended conformation
* Single type of repeating secondary structure

20
Q

What is the distribution of amino acids residues in a protein structure

A

Polypeptide chains fold so that hydrophobic side chains are buried and polar, as they don’t interact with the aqueous solution

Hydrophilic chains, charged chains are on the surface as they interact with the aqueous environment

21
Q

How do you think the distribution of amino acid residues may differ in a membrane protein?

A

?

22
Q

What happens when there is a disruption in protein structure

A

If proteins in a living cell are denatured,
this results in disruption of cell activity
and possibly cell death