Protein section 1

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Question 1 of 34

FOUR MAJOR FUNCTIONAL GROUPS:

Select one or more of the following:

Binding
Modification
Catalysis
Switching
Inhibition
Structural
Physiological

Explanation

Question 2 of 34

How is amide bond formed

Select one of the following:

dehydration
addition
hydrolysis
oxidation
reduction

Explanation

Question 3 of 34

The acidity of the carboxylic acid is due to....

Select one of the following:

stability of the carboxylate anion relative to the acid
the charge of the carboxylate residue
overall bonding
charge distribution

Explanation

Question 4 of 34

when the charge of the carboxylate resides two equivalent electronegative oxygens the structure is called

Select one of the following:

resonance form
protonated form
chiral form
assymetric form

Explanation

Question 5 of 34

pKa values vary somewhat depending on

Select one or more of the following:

the temperature of the solution
the precise molecular structure
the environment in which the acid-base chemistry is taking place.
how homogenous is the solution

Explanation

Question 6 of 34

The corresponding carboxylate anion is more stable in the presence of the adjacent, positively charged, ammonium ion, therefore

Select one of the following:

the carboxylic acid group of glycine is more acidic than a simple carboxylic acid since
the simple carboxylic acid is more acidic than the carboxylic acid group of glycine

Explanation

Question 7 of 34

The effect of environment on pKa is particularly important in non-polar conditions such as..

Select one of the following:

the interior of a protein
the outer part of the protein
the acidic part of the protein
the basic part of the protein

Explanation

Question 8 of 34

What stereoisomers predominate in nature

Select one of the following:

L-amino acids
D-amino acids

Explanation

Question 9 of 34

Into which groups can amino acids be divided

Select one or more of the following:

amino acids with hydrocarbon side chains
carboxylic acid side chains
amide side chains
acyclic with basic N containing side chains
hydroxyl functional groups
suphur containing side chains
nitrogen heterocycles and proline
hydrophilic side chains
hydrophobic side chain
phosphorus containing side chains

Explanation

Question 10 of 34

Which amino acid imparts unusual structural flexibility

Select one of the following:

Glycine
Serine
Proline
Guanine

Explanation

Question 11 of 34

What amino acid has two chiral centres due to the both of its α and β- carbons being asymmetric, and therefore has four possible stereoisomers.

Select one of the following:

Isoleucine
Valine
Glutamine
Cysteine

Explanation

Question 12 of 34

Confer negative charge on proteins because their side chains are ionised at pH 7, under physiological conditions acidic side chains exist as the conjugate base

Select one or more of the following:

aspartate
glutamate
arginine
histidine

Explanation

Question 13 of 34

The most basic of the 20 amino acids.

Select one of the following:

Histidine
Lysine
Arginine
Asparagine

Explanation

Question 14 of 34

The pKa of this protein is around pH 7 and thus at physiological pH it can act as either an acid or a base. This makes it especially important in acid-base catalysis and it has an important role to play in many enzymes. It also forms complexes with zinc in proteins which has importance for both structure and mechanism.

Select one of the following:

Histidine
Tryptophan
Methionine
Glutamine
Alanine

Explanation

Question 15 of 34

Click on each orange point and select the correct answer.

Fill in the blanks

Explanation

Question 16 of 34

Contains a non-polar methyl thioether group. This makes it one of the more hydrophobic amino acids

Select one of the following:

methionine
cysteine
serine
threonine

Explanation

Question 17 of 34

The hydroxymethyl group of this amino acid does not appreciably ionise at physiological pH. Essentially hydrophilic.

Select one of the following:

methionine
cysteine
serine
threonine

Explanation

Question 18 of 34

The side chain is somewhat hydrophobic, but also extremely reactive. It is polarisable and can lose its proton to bercome the thiolate anion. Can form disulphide bridges in proteins.

Select one of the following:

methionine
cysteine
serine
threonine

Explanation

Question 19 of 34

Has two chiral centres and thus can have four stereoisomers

Select one of the following:

methionine
cysteine
serine
threonine

Explanation

Question 20 of 34

Select from the dropdown lists to complete the text.

The formation of disulphide bonds in proteins is an important ( secondary, primary, teriary, quaternary ) structural feature. This helps to impart ( stability, acidity, reactivity, inertness ) and conformational rigidity to some proteins

Explanation

Question 21 of 34

This amino acid is unique in that its three carbon side chain is bonded to both the α carbon and the α amino group. The heterocyclic pyrrolidine ring created restricts the geometry of polypeptides.

Select one of the following:

proline
tyrosine
aspertate
valine

Explanation

Question 22 of 34

This amino acid has a hydroxyl function associated with the phenol ring. Acid base chemistry is facilitated as the ring enhances the stability of the conjugate base. It can sometimes act as an acid.

Select one of the following:

tyrosine
proline
tryptophan
phenyalanine

Explanation

Question 23 of 34

Select from the dropdown list to complete the text.

( Phe, Tyr and Trp, Ser, Thr and Cys, Val, Leu, Ile, Lys, Arg, His ) are all highly aromatic and can absorb UV light at 280nm. Proteins have an optical density at 280nm because of these side chains

Explanation

Question 24 of 34

Click on the orange point and select the correct answer.

drag the appropriate amino acid to the blank space

Explanation

Question 25 of 34

Select from the dropdown lists to complete the text.

The more ( hydrophobic, hydrophilic ) amino acids have a tendency to be sequestered away from the solvent towards the ( centre, inner part, outer part ) of protein molecules. This provides one of the major driving forces for protein ( folding, binding, inhibition )

Explanation

Question 26 of 34

Select from the dropdown lists to complete the text.

( Hydrophilic, hydrophobic ) residues tend to interact with the solvent more easily via ( hydrogen, covalent ) bonding and thus can be on the ( outside, inside ) of proteins.

Explanation

Question 27 of 34

Select from the dropdown lists to complete the text.

Under ( physiological, cellular ) conditions this effectively restricts the ( peptide, ionic ) bond to one of two configurations: cis or trans
To minimise steric crowding due to close proximity of bulky groups on th carbonyl carbon and the nitrogen the ( trans, cis ) form is favoursed, except where ( Proline, Histidine ) is involved.

Explanation

Question 28 of 34

Select from the dropdown lists to complete the text.

Proline has an ( alkyl, carboxyl ) chain rather than a ( hydrogen, oxygen ) atom as the ( second, third ) substituent on nitrogen
In amides containing proline the ( cis, trabs ) form is not dramatically disadvantaged
In proteins about ( 10%, 15%, 5% ) of all peptide bonds involving proline are cis.

Explanation

Question 29 of 34

Select from the dropdown list to complete the text.

THE SHAPE OF POLYPEPTIDES IS DEFINED BY ( ROTATION, SPIN, SIDE CHAIN, MOMENTUM ) ABOUT THE C-N AND C-C BONDS

Explanation

Question 30 of 34

Select from the dropdown lists to complete the text.

All atoms around the peptide bond lie in a ( planar, primary, cis, trans ) conformation.
This rotation is described by the torsion angles φ Phi between ( C-N, C-C ) and ψ Psi between ( C-C., C-N. )
If all psi and phi angles are the same the peptide assumes a ( repeated, saturated ) structure.
For certain combinations of angles this can take the form of a ( helical stucture (the alpha helix), coil structure ) or a beta-sheet structure.
Clearly the peptide structure exhibits ( flexibility, motitlity ) and this is important for the complex ( structure, binding ) of proteins.

Explanation

Question 31 of 34

What characteristic of atoms and groups of atoms limits the possible psi and phi torsion angles that the backbone of the polypeptide chain can adopt without causing protruding R groups to bump into each other.

Select one of the following:

The physical size
The chemical properties
The amount
The flexibility

Explanation

Question 32 of 34

The Ramachandran plot shows the allowed

Select one of the following:

psi and phi angles
carboxyl and amino groups
secondary structure of the protein
binding of the protein

Explanation

Question 33 of 34

Label the chemical structure

Drag an answer into the correct orange point.

Side chain

Alpha carbon

alpha-amino group

alpha-carboxylate

Explanation

Question 34 of 34

Amino acids with basic R groups

Select one or more of the following:

Lysine
Histidine
Arginine
Phenylalanine
Valine
Serine
Aspargine

Explanation

Check answer

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	Created by MrSujg over 8 years ago

1st year Biochemistry and molecular biology Quiz on Protein section 1, created by MrSujg on 19/11/2015.

Protein section 1

Question 1 of 34

FOUR MAJOR FUNCTIONAL GROUPS:

Select one or more of the following:

Explanation

Question 2 of 34

How is amide bond formed

Select one of the following:

Explanation

Question 3 of 34

The acidity of the carboxylic acid is due to....

Select one of the following:

Explanation

Question 4 of 34

when the charge of the carboxylate resides two equivalent electronegative oxygens the structure is called

Select one of the following:

Explanation

Question 5 of 34

pKa values vary somewhat depending on

Select one or more of the following:

Explanation

Question 6 of 34

The corresponding carboxylate anion is more stable in the presence of the adjacent, positively charged, ammonium ion, therefore

Select one of the following:

Explanation

Question 7 of 34

The effect of environment on pKa is particularly important in non-polar conditions such as..

Select one of the following:

Explanation

Question 8 of 34

What stereoisomers predominate in nature

Select one of the following:

Explanation

Question 9 of 34

Into which groups can amino acids be divided

Select one or more of the following:

Explanation

Question 10 of 34

Which amino acid imparts unusual structural flexibility

Select one of the following:

Explanation

Question 11 of 34

What amino acid has two chiral centres due to the both of its α and β- carbons being asymmetric, and therefore has four possible stereoisomers.

Select one of the following:

Explanation

Question 12 of 34

Confer negative charge on proteins because their side chains are ionised at pH 7, under physiological conditions acidic side chains exist as the conjugate base

Select one or more of the following:

Explanation

Question 13 of 34

The most basic of the 20 amino acids.

Select one of the following:

Explanation

Question 14 of 34

Select one of the following:

Explanation

Question 15 of 34

Click on each orange point and select the correct answer.

Fill in the blanks

Explanation

Question 16 of 34

Contains a non-polar methyl thioether group. This makes it one of the more hydrophobic amino acids

Select one of the following:

Explanation

Question 17 of 34

The hydroxymethyl group of this amino acid does not appreciably ionise at physiological pH. Essentially hydrophilic.

Select one of the following:

Explanation

Question 18 of 34

The side chain is somewhat hydrophobic, but also extremely reactive. It is polarisable and can lose its proton to bercome the thiolate anion. Can form disulphide bridges in proteins.

Select one of the following:

Explanation

Question 19 of 34

Has two chiral centres and thus can have four stereoisomers

Select one of the following:

Explanation

Question 20 of 34

Select from the dropdown lists to complete the text.

Explanation

( Phe, Tyr and Trp, Ser, Thr and Cys, Val, Leu, Ile, Lys, Arg, His ) are all highly aromatic and can absorb UV light at 280nm. Proteins have an optical density at 280nm because of these side chains

( Hydrophilic, hydrophobic ) residues tend to interact with the solvent more easily via ( hydrogen, covalent ) bonding and thus can be on the ( outside, inside ) of proteins.

THE SHAPE OF POLYPEPTIDES IS DEFINED BY ( ROTATION, SPIN, SIDE CHAIN, MOMENTUM ) ABOUT THE C-N AND C-C BONDS