Protein folding determines the shape of the protein, and thus what it does, because it is the shape of the protein which enables it to perform its function. For example, enzymes need to have exactly the right shape to fit with the molecules they are working with to catalyze them. Also, hemoglobin is specifically folded with four pocket like areas to allow oxygen to attach to it. The shape of the protein is specific to the function that it is performing, and is different for each protein. If there is even a slight change in the make up of the protein, or a mutation (the amino acids are messed up) then the protein will fold differently. Even a slight change in the composition of the protein can disable the protein from properly performing the function which it is meant to do.
Type your answer here... Which of these organelles is responsible for folding proteins in the cell?
No! Lysosomes hydrolyze cellular material ( digest it ). The actual folding of proteins is done by a class of proteins called chaperons. Two types: chaperons and chaparonins. Also proteins fold naturally by the arrangement of the R groups on the constituent amino acids.
Chaperone proteins assist in the correct folding of newly synthesized proteins. They also help prevent misfolded or aggregated proteins from forming and aid in the transport of proteins within the cell. Additionally, chaperones can facilitate the refolding of denatured proteins under stress conditions.
Chaperonins provide a good environment to facilitate protein folding.
Proteins do it all the time, its called folding.
chaperonins
Type your answer here... Which of these organelles is responsible for folding proteins in the cell?
23 =)
23 =)
No! Lysosomes hydrolyze cellular material ( digest it ). The actual folding of proteins is done by a class of proteins called chaperons. Two types: chaperons and chaparonins. Also proteins fold naturally by the arrangement of the R groups on the constituent amino acids.
I don't have a clue, what do you think?
The rough ER is the site of protein modification and folding of proteins, if they need folding. The smooth ER is the site of lipid and steroid synthesis.
The rough ER is the site of protein modification and folding of proteins, if they need folding. The smooth ER is the site of lipid and steroid synthesis.
Chaperone proteins assist in the correct folding of newly synthesized proteins. They also help prevent misfolded or aggregated proteins from forming and aid in the transport of proteins within the cell. Additionally, chaperones can facilitate the refolding of denatured proteins under stress conditions.
Chaperonins provide a good environment to facilitate protein folding.
Proteins do it all the time, its called folding.
These barrel shaped and lidded proteins ( not to be confused with chaperones ) are tasked with the proper folding of misshapen polypeptide chains/proteins in the cytosol