Introduction to protein structure Flashcards

1
Q

Sketch a two amino acids linked with a peptide bond and identify the amino terminus, carboxyl terminus and side chains

A

add pic

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2
Q

Define Primary Sequence

A

is the linear sequence of amino acids that make up the proteins

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3
Q

Define secondary structure

A

Secondary structure is the folding of the polypeptide chain due to hydrogen bonding into an alpha helix structure, resembling a coiled spring, or a beta pleated sheet.

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4
Q

Define tertiary structure

A

The final 3D structure of a protein, entailing the shaping of a secondary structure.

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5
Q

Define quanternary structure

A

Is the 3D structure of a multimeric protein composed of several subunits (polypeptide chains).

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6
Q

Draw an alpha helix

A

add pic

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7
Q

What happens when proline is added to a polypeptide chain

A

When proline is joined to a polypeptide chain, the NH group of the amino acid is lost. This prevents the side chain from hydrogen bonding with C=O groups of another residue within the helix, thereby distorting the helical conformation, putting a ‘kink’ into it

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8
Q

Draw a beta pleated sheet

A

add pic In the b-pleated sheet, the NH and C=O groups point out at right angles to the line of the backbone. This almost two dimensional sheet is pleated, like the bellows of an accordion

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9
Q

What type of bond stabalises beta pleated sheet and alpha helix

A

Hydrogen bonds

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10
Q

Name the bonds that hold proteins together

A

Covalent

Hydrogen

Ionic

Van der Waals Forces

Hydrophobic Interactions

Usually hydrophobic side chains are packed in the interior. This creates a hydrophobic core and a hydrophiic surface to most proteins

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