Protein Structure Flashcards

(28 cards)

1
Q

Describe the structure of an amino acid

A
Amino group
Carboxyl group
Hydrogen atom
R group
N-C-C
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2
Q

How many amino acids are used in the body?

A

20

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3
Q

What are the 9 essential amino acids?

A
Isoleucine (if)
Leucine (learnt)
Threonine (this)
Histidine (huge)
Lysine (list)
Methionine (may)
Phenylalanine (prove)
Valine (valuable)
Tryptophan
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4
Q

What chemical properties are amino acids classified from?

A

Hydrophobic/hydrophilic
Polar/non-polar
Acidic/basic/neutral

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5
Q

What physical properties are amino acids classified from?

A

Aliphatic

Aromatic

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6
Q

What is an amino acid residue?

A

What remains of an amino acid after it has been joined by a peptide bond to form a protein

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7
Q

What does a lower pK indicate?

A

More likely to dissociate and stronger the acid

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8
Q

What causes the group on amino acid to be protonated?

A

If the pH of the solution < the pK value

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9
Q

What causes the group on an amino acid to be deprotonated?

A

If the pH of the solution > the pK value

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10
Q

Describe primary protein structure

A

Linear amino acid sequence of polypeptide chain
Covalent bonds hold it together
Angles determine conformation of peptide backbone and hence ‘fold’ of protein

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11
Q

Describe secondary protein structure

A

Local spatial arrangement of polypeptide backbone

Alpha helix/beta sheets

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12
Q

Describe tertiary protein structure

A

Overall 3D configuration of protein

Spatial arrangement of amino acids far apart in protein sequence

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13
Q

Describe quaternary protein structure

A

Association between different polypeptides to from a multi-subunit protein

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14
Q

What are the properties of peptide bonds?

A
Produce water when formed
Planar
Rigid
Trans conformation
Bonds on either side of peptide bond free to rotate
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15
Q

Why are amino acids important in proteins?

A

Amino acid sequence determines the way in which polypeptide chain folds and physical characteristics of protein

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16
Q

What is an isoelectric point?

A

The pH at which there is no overall net charge

17
Q

What is the pI of basic proteins?

A

pI >7 as it contains many positively charged amino acids

18
Q

What is the pI ion acidic proteins?

A

pI < 7 as they contain many negatively charged amino acids

19
Q

How many amino acids in peptides or oligopeptides?

20
Q

How many amino acids in polypeptides or proteins?

21
Q

What are conjugated proteins?

A

Proteins that contain covalently linked chemical components in addition to amino acids
E.g. prosthetic group - haem or iron

22
Q

What are the bonds present at each level of protein structure?

A

Primary: covalent (peptide)
Secondary: H bonds
Tertiary: covalent (disulphide), ionic, H bonds, London forces, hydrophobic
Quaternary: covalent (disulphide), ionic, H bonds, London forces, hydrophobic

23
Q

Describe fibrous proteins

A

Role is to support, shape and protect
Long strands or sheets
Single type of repeating secondary structure
E.g. collagen

24
Q

Describe globular proteins

A
Role is catalysis and regulation
Compact
Several types of secondary structure
Form enzymes and transporter proteins
E.g. carbonic anhydrase
25
Describe the structure of collagen
Triple helical arrangement of collagen chains Contain gly-x-y repeating sequence Hydrogen bonds stabilise interactions between chains Collagen fibrils formed from covalently cross-linked collagen molecules
26
What are motifs in globular proteins?
Folding patterns containing one or more elements of secondary structures E.g. beta-alpha-beta loop
27
What are domains in globular proteins?
Part of a polypeptide chain that fold into a distinct shape, often has a specific functional role
28
What is protein denaturation?
Losing its negative state Disruption of protein structure Caused by breaking of forces that hold proteins together E.g. by heat, pH, or detergents/organic solvents