4.7 Amino acids, peptides & proteins Flashcards

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1
Q

what is an a-amino acid?

A

a-amino acids are organic molecules containing a carboxylic acid group and amine group bonded to the same carbon atom

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2
Q

displayed formula structure of an a-amino acid representing the side chain w/ R

A

HOOC-CH-R1-NH2

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3
Q

Which amino acid is the only amino acid that is not chiral?

A

aminoethanoic acid (glycine): the R group on aminoethanoic acid is just a hydrogen atom so the carbon is not bonded to 4 diff grps.

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4
Q

why are all amino acids (except glycine) chiral molecules?

A

all amino acids, except glycine, contain a chiral carbon atom bonded to four separate groups, it is bonded to an amino group, a carboxylic group a hydrogen atom and an R group

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5
Q

how are amino acids amphoteric?

A

amino acids are amphoteric meaning they have both acidic and basic properties, they have a basic amino grp and an acidic carboxylic grp

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6
Q

what is a zwitterion?

A

a zwitterion is a dipolar ion which means it has a positive charge in one part of the molecule and a negative part in another part on the molecule

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7
Q

General displayed stricture of an amino acid zwitterion

A

N+H3-CRH-CO(minus) =O

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8
Q

What happens when an alkali is added to an amino acid zwitterion?

A

The NH3+ grp donates a hydrogen ion to OH(minus) ions of the alkali to form water, the organic compound is no longer zwitterion as it only contains a -ve charge

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9
Q

What happens when an acid is added to an amino acid zwitterion?:

A

The COO- grp accepts a hydrogen ion from the acid, the organic compound is no longer a zwitterion as it only contains a +ve charge

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10
Q

General displayed structure of an amino acid in acidic conditions

A

N+H3-CRH-COH=O

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11
Q

General displayed structure of an amino acid in alkaline conditions

A

NH2-CRH-CO(minus)=O

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12
Q

Why do amino acids have relatively high melting points?

A

In the solid state the zwitterion is the usual form that an amino acid exists in, this means there are strong ionic attractions between neighbouring zwitterions in solid so a large amount of energy required to break the ionic attractions

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13
Q

explain the solubility of amino acids in water

A

amino acids are generally soluble in water because strong ionic attractions form between the zwitterions and polar water molecules

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14
Q

how does a peptide bond form?

A

a peptide bond forms during condensation reactions between two amino acids, a water molecule is lost

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15
Q

what is the difference between a dipeptide and a polypeptide?

A

dipeptide is formed from 2 amino acids, polypeptide formed from more than 2 amino acids

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16
Q

structure of peptide linkage

A

-C(=Oabve)-N(-Habve)- (+H2O in condensation rctns)

17
Q

how to polypeptides lead to protein formation?

A

polypeptides are chains of more than two amino acids joined together by peptide links, when the chain becomes very long, they can fold into proteins

18
Q

what does the primary structure of a protein involve?

A

the primary structure of a protein is the sequence of amino acids which make up the polypeptide chain

19
Q

what does the secondary structre of a protein involve?

A

the protein chain has peptide links which can form hydrogen bonds with each other leading to two possible shapes of the chain, a-helix spiral, B-pleated sheet, both stabilised by hydrogen bonding

20
Q

what does the tertiary structure of a protein involve?

A

the tertiary structure related to the extra bonds which can form between diff parts of the polypeptide chain, determining how the a-helices or B-pleated sheets of protein fold wrt each other, the types of extra bonds include, ionic & hydrogen bonds and disulphide bridges

21
Q

give examples of how proteins are essential for living systems:

A

-proteins are important for structural functions in living organisms, nails, feathers, skin, collagen are all made up of protein
-enzymes are proteins that are biological catalysts that speed up chemical rctns in the body
- some hormones are proteins e.g. insulin