B.2 Proteins and enzymes

Proteins are polymers of amino acids.

Glycine is one of the amino acids in the primary structure of hemoglobin.

State the type of bonding responsible for the α-helix in the secondary structure.

Proteins are polymers of amino acids.

Glycine is one of the amino acids in the primary structure of hemoglobin.

State the type of bonding responsible for the α-helix in the secondary structure.

Proteins are polymers of amino acids.

Glycine is one of the amino acids in the primary structure of hemoglobin.

State the type of bonding responsible for the α-helix in the secondary structure.

Proteins are polymers of amino acids.

The mixture is composed of glycine, $\mathrm{Gly}$, and isoleucine, $\mathrm{Ile}$. Their structures can be found in section 33 of the data booklet.

Deduce, referring to relative affinities and ${\mathrm{R}}_{\mathrm{f}}$, the identity of A1.

Proteins are polymers of amino acids.

The mixture is composed of glycine, $\mathrm{Gly}$, and isoleucine, $\mathrm{Ile}$. Their structures can be found in section 33 of the data booklet.

Deduce, referring to relative affinities and ${\mathrm{R}}_{\mathrm{f}}$, the identity of A1.

Proteins are polymers of amino acids.

The mixture is composed of glycine, $\mathrm{Gly}$, and isoleucine, $\mathrm{Ile}$. Their structures can be found in section 33 of the data booklet.

Deduce, referring to relative affinities and ${\mathrm{R}}_{\mathrm{f}}$, the identity of A1.

Proteins are polymers of amino acids.

Glycine is one of the amino acids in the primary structure of hemoglobin.

State the type of bonding responsible for the α-helix in the secondary structure.

Proteins are polymers of amino acids.

Glycine is one of the amino acids in the primary structure of hemoglobin.

State the type of bonding responsible for the α-helix in the secondary structure.

Proteins are polymers of amino acids.

Glycine is one of the amino acids in the primary structure of hemoglobin.

State the type of bonding responsible for the α-helix in the secondary structure.

Proteins are polymers of amino acids.

A paper chromatogram of two amino acids, A1 and A2, is obtained using a non-polar solvent.

© International Baccalaureate Organization 2020.

Determine the ${\mathrm{R}}_{\mathrm{f}}$ value of A1.

Proteins are polymers of amino acids.

A paper chromatogram of two amino acids, A1 and A2, is obtained using a non-polar solvent.

© International Baccalaureate Organization 2020.

Determine the ${\mathrm{R}}_{\mathrm{f}}$ value of A1.

Proteins are polymers of amino acids.

A paper chromatogram of two amino acids, A1 and A2, is obtained using a non-polar solvent.

© International Baccalaureate Organization 2020.

Determine the ${\mathrm{R}}_{\mathrm{f}}$ value of A1.

Draw the structures of the main form of glycine in buffer solutions of pH 1.0 and 6.0.

The pK_a of glycine is 2.34.

Draw the structures of the main form of glycine in buffer solutions of pH 1.0 and 6.0.

The pK_a of glycine is 2.34.

Draw the structures of the main form of glycine in buffer solutions of pH 1.0 and 6.0.

The pK_a of glycine is 2.34.

Outline how the amino acids may be identified from a paper chromatogram.

Outline how the amino acids may be identified from a paper chromatogram.

Outline how the amino acids may be identified from a paper chromatogram.

Draw a circle around the functional group formed between the amino acids and state its name.

Name:

Draw a circle around the functional group formed between the amino acids and state its name.

Name:

Draw a circle around the functional group formed between the amino acids and state its name.

Name:

A mixture of phenylalanine and aspartic acid is separated by gel electrophoresis with a buffer of pH = 5.5.

Deduce their relative positions after electrophoresis, annotating them on the diagram. Use section 33 of the data booklet.

A mixture of phenylalanine and aspartic acid is separated by gel electrophoresis with a buffer of pH = 5.5.

Deduce their relative positions after electrophoresis, annotating them on the diagram. Use section 33 of the data booklet.

A mixture of phenylalanine and aspartic acid is separated by gel electrophoresis with a buffer of pH = 5.5.

Deduce their relative positions after electrophoresis, annotating them on the diagram. Use section 33 of the data booklet.

Draw a circle around the functional group formed between the amino acids and state its name.

Name: 

Draw a circle around the functional group formed between the amino acids and state its name.

Name: 

Draw a circle around the functional group formed between the amino acids and state its name.

Name: 

A mixture of phenylalanine and aspartic acid is separated by gel electrophoresis with a buffer of pH = 5.5.

Deduce their relative positions after electrophoresis, annotating them on the diagram. Use section 33 of the data booklet.

A mixture of phenylalanine and aspartic acid is separated by gel electrophoresis with a buffer of pH = 5.5.

Deduce their relative positions after electrophoresis, annotating them on the diagram. Use section 33 of the data booklet.

A mixture of phenylalanine and aspartic acid is separated by gel electrophoresis with a buffer of pH = 5.5.

Deduce their relative positions after electrophoresis, annotating them on the diagram. Use section 33 of the data booklet.

Compare and contrast the bonding responsible for the two secondary structures.

One similarity:

One difference:

Compare and contrast the bonding responsible for the two secondary structures.

One similarity:

One difference:

Compare and contrast the bonding responsible for the two secondary structures.

One similarity:

One difference:

The isoelectric point of amino acids is the intermediate pH at which an amino acid is electrically neutral.

Suggest why Asp and Phe have different isoelectric points.

The isoelectric point of amino acids is the intermediate pH at which an amino acid is electrically neutral.

Suggest why Asp and Phe have different isoelectric points.

The isoelectric point of amino acids is the intermediate pH at which an amino acid is electrically neutral.

Suggest why Asp and Phe have different isoelectric points.

Explain why a change in pH affects the tertiary structure of an enzyme in solution.

Explain why a change in pH affects the tertiary structure of an enzyme in solution.

Explain why a change in pH affects the tertiary structure of an enzyme in solution.

Draw the structural formula of a dipeptide containing the residues of valine, Val, and asparagine, Asn, using section 33 of the data booklet.

Draw the structural formula of a dipeptide containing the residues of valine, Val, and asparagine, Asn, using section 33 of the data booklet.

Draw the structural formula of a dipeptide containing the residues of valine, Val, and asparagine, Asn, using section 33 of the data booklet.

Deduce the strongest intermolecular forces that would occur between the following amino acid residues in a protein chain.

Deduce the strongest intermolecular forces that would occur between the following amino acid residues in a protein chain.

Deduce the strongest intermolecular forces that would occur between the following amino acid residues in a protein chain.

Draw the dipeptide represented by the formula Ala-Gly using section 33 of the data booklet.

Draw the dipeptide represented by the formula Ala-Gly using section 33 of the data booklet.

Draw the dipeptide represented by the formula Ala-Gly using section 33 of the data booklet.

Outline why amino acids have high melting points.

Outline why amino acids have high melting points.

Outline why amino acids have high melting points.

Some proteins form an α-helix. State the name of another secondary protein structure.

Some proteins form an α-helix. State the name of another secondary protein structure.

Some proteins form an α-helix. State the name of another secondary protein structure.

Compare and contrast the bonding responsible for the two secondary structures.

One similarity:

One difference:

Compare and contrast the bonding responsible for the two secondary structures.

One similarity:

One difference:

Compare and contrast the bonding responsible for the two secondary structures.

One similarity:

One difference:

Explain why an increase in temperature reduces the rate of an enzyme-catalyzed reaction.

Explain why an increase in temperature reduces the rate of an enzyme-catalyzed reaction.

Explain why an increase in temperature reduces the rate of an enzyme-catalyzed reaction.

Some proteins form an α-helix. State the name of another secondary protein structure.

Some proteins form an α-helix. State the name of another secondary protein structure.

Some proteins form an α-helix. State the name of another secondary protein structure.

Explain why an increase in temperature reduces the rate of an enzyme-catalyzed reaction.

Explain why an increase in temperature reduces the rate of an enzyme-catalyzed reaction.

Explain why an increase in temperature reduces the rate of an enzyme-catalyzed reaction.

Draw the structure of the dipeptide Asp–Phe using section 33 of the data booklet.

Draw the structure of the dipeptide Asp–Phe using section 33 of the data booklet.

Draw the structure of the dipeptide Asp–Phe using section 33 of the data booklet.

Draw the structure of the dipeptide Asp–Phe using section 33 of the data booklet.

Draw the structure of the dipeptide Asp–Phe using section 33 of the data booklet.

Draw the structure of the dipeptide Asp–Phe using section 33 of the data booklet.

Proteins are polymers of amino acids. A paper chromatogram of two amino acids, A1 and A2, is obtained using a non-polar solvent.

© International Baccalaureate Organization 2020.

Determine the ${\mathrm{R}}_{\mathrm{f}}$ value of A1.

Proteins are polymers of amino acids. A paper chromatogram of two amino acids, A1 and A2, is obtained using a non-polar solvent.

© International Baccalaureate Organization 2020.

Determine the ${\mathrm{R}}_{\mathrm{f}}$ value of A1.

Proteins are polymers of amino acids. A paper chromatogram of two amino acids, A1 and A2, is obtained using a non-polar solvent.

© International Baccalaureate Organization 2020.

Determine the ${\mathrm{R}}_{\mathrm{f}}$ value of A1.

Proteins are polymers of amino acids.

The mixture is composed of glycine, $\mathrm{Gly}$, and isoleucine, $\mathrm{Ile}$. Their structures can be found in section 33 of the data booklet.

Deduce, referring to relative affinities and ${\mathrm{R}}_{\mathrm{f}}$, the identity of A1.

Proteins are polymers of amino acids.

The mixture is composed of glycine, $\mathrm{Gly}$, and isoleucine, $\mathrm{Ile}$. Their structures can be found in section 33 of the data booklet.

Deduce, referring to relative affinities and ${\mathrm{R}}_{\mathrm{f}}$, the identity of A1.

Proteins are polymers of amino acids.

The mixture is composed of glycine, $\mathrm{Gly}$, and isoleucine, $\mathrm{Ile}$. Their structures can be found in section 33 of the data booklet.

Deduce, referring to relative affinities and ${\mathrm{R}}_{\mathrm{f}}$, the identity of A1.

Proteins are polymers of amino acids.

Describe how the tertiary structure differs from the quaternary structure in hemoglobin.

Proteins are polymers of amino acids.

Describe how the tertiary structure differs from the quaternary structure in hemoglobin.

Proteins are polymers of amino acids.

Describe how the tertiary structure differs from the quaternary structure in hemoglobin.