Protein structure, binding and conformational changes 1.2 Flashcards

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1
Q

What are the 4 animo acid R groups

A

Basic (positively charged) , acidic (negatively charged), polar and hydrophobic

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2
Q

What gives amino acids their specific shape and properties

A

The R group

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3
Q

What is a basic amino acid R group

A

Generally have NH2 which allows them to accept a proton (H+) and become positively charged and strongly hydrophilic as a consequence

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4
Q

What is an acidic amino acid R group

A

They have a carboxylic acid group which’s allows them to donate a proton, this causes them to become negatively charged and strongly hydrophilic

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5
Q

What are polar amino acid R groups

A

Hydrophilic as they form weak hydrogen bonds with water molecules. They have a slightly positive and slightly negative side and all have NITROGEN or OXYGEN or SULFUR on their R side chain

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6
Q

What are hydrophobic amino acid R groups

A

Typical non polar R groups are: hydrocarbons
They do not become charged and cannot form hydrogen bonds with water

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7
Q

What is the primary protein structure

A

The order in which the amino acids are synthesised during translation into the polypeptide

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8
Q

What bond joins amino acids together

A

Peptide bond

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9
Q

What reaction forms the peptide bond

A

Condensation reaction- between OH of COOH and H of NH2

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10
Q

What is the secondary protein structure

A

Hydrogen bonding along the backbone of the protein strand

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11
Q

What are the secondary protein structure regions called

A

A-helices, parallel/anti-parallel B pleated sheets, turns

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12
Q

When does the alpha helix occur

A

Hydrogen bonds form between every fourth peptide bond

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13
Q
A
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