Protein Folding

What is the difference between the primary and tertiary structure of proteins?

• primary is local folding, tertiary is overall 3D folding

• primary is not folded, tertiary is overall 3D folding

• primary is overall 3D folding, tertiary is local folding

• primary is overall 3D folding, tertiary is not folded

Proteins are usually folded in the _________ and tagged in the __________.

• nucleus, ribosome

• ribosome, endoplasmic reticulum

• Golgi apparatus, endoplasmic reticulum

• endoplasmic reticulum, Golgi apparatus

Which of the following is most likely to determine the function of a protein?

• what part of the cell needs it

• where it is located at any point in time

• its structure based on the introns in the genes

• its structure based on the biochemical properties of amino acids

Tags

NGSS.HS-LS1-1

What is the name of bonds that hold amino acids together?

• Peptide bonds

• Protein bonds

• Hydrogen bonds

• Phosphodiester bonds

The function of the rough ER is to

• Produce and folding proteins

• Produce and folding carbohydrates

• Produce and folding lipids

• Produce and folding Nucleic acids

What is the special type of bond that forms between two amino acids?

• hydrogen bond

• ionic bond

• peptide bond

What is the primary driving force behind protein folding?

• Hydrophobic interactions

• Hydrogen bonding

• Ionic interactions

• Van der Waals forces

Which of the following structures is formed first during protein folding?

• Primary structure

• Secondary structure

• Tertiary structure

• Quaternary structure

What is the role of chaperone proteins in protein folding?

• They assist in the correct folding of proteins

• They degrade misfolded proteins

• They transport proteins to the Golgi apparatus

• They modify proteins post-translation

Which experimental technique is commonly used to study protein folding?

• X-ray crystallography

• NMR spectroscopy

• Mass spectrometry

• Western blotting