Folding of a protein is a thermodynamically favored process despite the fact tha
ID: 86304 • Letter: F
Question
Folding of a protein is a thermodynamically favored process despite the fact that entropy for the polypeptide itself decreases. Choose the letters of the sentences which explain and describe how protein folding becomes favorable. a) Conformational entropy is unfavorable with protein folding. b) Conformational entropy is favorable with protein folding. c) A positive Delta H can be obtained by noncovalent interactions (H bonding, salt bridge formation, dispersion forces) d) A negative Delta H can be obtained by noncovalent interactions (H bonding, salt bridge formation, dispersion forces) e) A positive Delta S can be obtained by internalizing hydrophobic side chains. f) A negative Delta S can be obtained by internalizing hydrophobic side chains. g) Internalizing hydrophobic side chains gives a positive Delta S by breaking water clathrates around hydrophobic side chains. h) Internalizing hydrophobic side chains gives a negative Delta S by breaking water clathrates around hydrophobic side chains. Collagen is derived from precursor proteins that are modified after translation. Identify the precursors, explain what the modifications are and if/how they affect the final structure of collagen. a) Protein is translated on the lysosome. b) Protein is translated on the ribosome. c) Protein is hydroxylated and then sugars are added to serine sidechains. d) Protein is hydroxylated and then sugars are added to lysine sidechains. e) Moves into cytosol, forms triple helix and globular domains and becomes procollagen f) Moves into extracellular space, forms triple helix and becomes procollagen g) Does not remove N and C termini, crosslinks and becomes collagen in extracellular space. h) Removal of N and C terminal domains and becomes tropocollagen in extracellular space. i) Tropocollagen crosslinks and becomes collagen.Explanation / Answer
2) The folded structure of protein is more stable state than the unfolded state and this mainly because of the non-polar hydrophobic side chains. The entropy and enthalpy of the folded state is low. Prtein folding could be described as an entropy driven process.
3) Collagen could be formed proline precursors, but it could also be formed from from linking of tropocollagen which is formed from procollagen.