Protein Folding- The Basics

1

Define Protein Folding

1

Which structure of a protein shows biological activity?

1

Which of the following occurs to ALL proteins?

1

Which of the following are covalent modifications of the polypeptide chain?

1

Folding corresponds to a hierarchy of protein structure

1

Put the following in Order
A -Unfolded
B - Nucleation
C - Secondary Structure
D - Domain
E - Active Oligomer
F - Inactive Oligomer
G - Supersecondary Structure
H - Folded Monomer

1

What is meant by the 'Thermodynamic Hypothesis of Protein Folding'

1

The Kinetic Hypothysis suggests that there is a specific folding pathway for each protein- protein folding is not random

1

Describe the features of the RNAase Refolding experiment?

1

How do we know the RNAase really was denatured during the experiment?

1

Which of the following are conditions for In Vitro Refolding (Like in the RNAase experiment)?

1

What type of amino acid is being shown ere?

1

Trans formations are less stable due to their steric hindrance

1

Proline is added to an amino acid chain exclusively in what form?

1

Which of the following proteins converts cis isomers to their trans form?

1

In the Cis form, the clash of functional groups around the alpha carbon is much greater due to steric hindrance

1

What type of bond is being shown here?

1

The previous amino acid to proline experiences steric hindrance in either proline conformation

1

Cis proline has _ energy than/to trans proline

1

The two cystine molecules that bind together are known as what?

1

Proteins with di-sulphide bonds are most likely to be found where?

1

Phosphorylation occurs on which residues?

1

Pro-sequences are found at the C-terminus

1

The Pro-sequence is also known as

1

Which proteins will have a pro-sequence?

1

The protein with a pro-sequence will auto-cleave it before folding correctly

1

What is co-operativity in protein folding?

1

What does the Hydrophobic Zipper Model suggest?

Structural Basis for Biological Function (Protein Folding) Quiz am Protein Folding- The Basics, erstellt von gina_evans0312 am 19/12/2013.

Protein Folding- The Basics

Protein Folding- The Basics

Define Protein Folding

Which structure of a protein shows biological activity?

Which of the following occurs to ALL proteins?

Which of the following are covalent modifications of the polypeptide chain?

Folding corresponds to a hierarchy of protein structure

Put the following in Order A -Unfolded B - Nucleation C - Secondary Structure D - Domain E - Active Oligomer F - Inactive Oligomer G - Supersecondary Structure H - Folded Monomer

What is meant by the 'Thermodynamic Hypothesis of Protein Folding'

The Kinetic Hypothysis suggests that there is a specific folding pathway for each protein- protein folding is not random

Describe the features of the RNAase Refolding experiment?

How do we know the RNAase really was denatured during the experiment?

Which of the following are conditions for In Vitro Refolding (Like in the RNAase experiment)?

What type of amino acid is being shown ere?

Trans formations are less stable due to their steric hindrance

Proline is added to an amino acid chain exclusively in what form?

Which of the following proteins converts cis isomers to their trans form?

In the Cis form, the clash of functional groups around the alpha carbon is much greater due to steric hindrance

What type of bond is being shown here?

The previous amino acid to proline experiences steric hindrance in either proline conformation

Cis proline has _ energy than/to trans proline

Put the following in Order
A -Unfolded
B - Nucleation
C - Secondary Structure
D - Domain
E - Active Oligomer
F - Inactive Oligomer
G - Supersecondary Structure
H - Folded Monomer