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NUT1004 > Amino Acids > Flashcards

Amino Acids Flashcards

1
Q

How many amino acids do proteins typically contain

A

50-2000 AA residues

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2
Q

In neutral solution which end of the AA is positively charged

A

Amino group

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3
Q

In neutral solution which end of the AA is negatively charged

A

Carboxyl group

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4
Q

What is a zwitterion and why are AA zwitterions

A

Ends are oppositely charged in solution

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5
Q

What is the N-terminal of the polypeptide

A

The amino group first AA in chain

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6
Q

What is the C-terminal of the polypeptide

A

Carboxyl group of last AA in chain

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7
Q

How many proteinaceous AAs are there

A

20

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8
Q

What is the common core of AA

A

Central C joined to H-atom

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9
Q

What is a chiral molecule

A

all four sites are occupied by different groups, so two versions of the molecule can exist as the same atoms connected in the same sequence but with different positions

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10
Q

Why are chiral molecules enantiomers

A

Mirror image versions of each other than cannot be superimposed on eachother

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11
Q

How are chiral molecules distinguished

A

Named D and L isomers of molecule

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12
Q

What determines the character/behaviour of an amino acid

A

The R group/side chain

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13
Q

How do side chains determine AA behaviour (6 ways)

A

Vary in size, shape, charge, hydrogen bonding capacity, hydrophobicity and chemical reactivity

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14
Q

What are the 5 main groups of amino acids

A

Hydrophobic (with nonpolar aliphatic), hydrophobic (with aromatic), polar (with neutral R groups and uneven charge distribution), positively charged (with +charged R groups at pH 7), negatively charged (with -charged R groups at physiological pH)

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15
Q

What does aliphatic mean

A

No aromatic rings present

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16
Q

Which version of AA are found in proteins (D or L)

A

L isomer

17
Q

Named the 7 hydrophobic with non polar aliphatic AAs

A

Glycine, alanine, proline, valine, leucine, isoleucine, methionine

18
Q

Which AA is a chiral (no D or L form) and why

A

Glycine- has hydrogen as R group (simplest AA)

19
Q

What are the features of hydrophobic with nonpolar aliphatic R group AAS

A

Mainly hydrocarbon side chains, hydrophobic

20
Q

Name the 2 hydrophobic with nonpolar aromatic side chains AAs

A

Phenylalanine and tryptophan

21
Q

What are the properties of hydrophobic with non polar aromatic R group AAs

A

Large, hydrophobic

22
Q

How does the large size of hydrophobic with non polar aromatic R group AA impact protein structure

A

Take up more space in the polypeptide so food is less tight

23
Q

What does aromatic means

A

Aromatic benzene-type rings present

24
Q

Why are covalent bonds polar

A

Electrons unequally shared

25
Q

Name the polar, with neutral R groups but uneven charge distribution AAs

A

Serine, threonine, cysteine, tyrosine, asparagine, glutamine

26
Q

What are the properties of polar, with neutral R groups but uneven charge distribution AAs

A

Side chains with polarity due to uneven share of electrons, more hydrophilic R groups than nonpolar, form H bonds with water

27
Q

What does the -SH group in cysteine mean for a polypeptide

A

Pairs of SH groups close together may form a disulphide bond linking parts of the polypeptide together

28
Q

Name the positively charged R group AAs

A

Lysine, Arginine, Histidine

29
Q

What are the characteristics of positively charged R group AAs

A

Side chains with positive charge at pH 7, hydrophilic R groups due to ionic charge

30
Q

What feature of Histidine makes it a useful component of active sites

A

Able to bind to or release H+ near physiological pH so can serve as a proton donor/ acceptor

31
Q

Name the negatively charged R group AAs

A

Aspartate, Glutamate

32
Q

Name the features of negatively charged R group AAs

A

Posses a Carboxyl group in the side chain, negatively charged at physiological pH, ionic charge makes R group hydrophilic, side chains can be important proton acceptors in proteins

NUT1004 (14 decks)

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