Here is an interesting article on Protein Structures and their related Amino Acid Sequences.
https://www.nature.com/scitable/topicpage/protein-structure-14122136
What caught my attention was the Chaperone Protein:
How Do Proteins Arrive at Their Final Shapes?
"In theory, once their constituent amino acids are strung together, proteins attain their final shapes without any energy input. In reality, however, the cytoplasm is a crowded place, filled with many other macromolecules capable of interacting with a partially folded protein. Inappropriate associations with nearby proteins can interfere with proper folding and cause large aggregates of proteins to form in cells. Cells therefore rely on so-called chaperone proteins to prevent these inappropriate associations with unintended folding partners.
Chaperone proteins surround a protein during the folding process, sequestering the protein until folding is complete. For example, in bacteria, multiple molecules of the chaperone GroEL form a hollow chamber around proteins that are in the process of folding. Molecules of a second chaperone, GroES, then form a lid over the chamber. Eukaryotes use different families of chaperone proteins, although they function in similar ways.
Chaperone proteins are abundant in cells. These chaperones use energy from ATP to bind and release polypeptides as they go through the folding process. Chaperones also assist in the refolding of proteins in cells. Folded proteins are actually fragile structures, which can easily denature, or unfold. Although many thousands of bonds hold proteins together, most of the bonds are noncovalent and fairly weak. Even under normal circumstances, a portion of all cellular proteins are unfolded. Increasing body temperature by only a few degrees can significantly increase the rate of unfolding. When this happens, repairing existing proteins using chaperones is much more efficient than synthesizing new ones. Interestingly, cells synthesize additional chaperone proteins in response to "heat shock." "
I wonder of I can get Jano in here to comment on these "Chaperone Proteins", and if they may negate the ability of an Amino Acid chain to be folded incorrectly.
https://www.nature.com/scitable/topicpage/protein-structure-14122136
What caught my attention was the Chaperone Protein:
How Do Proteins Arrive at Their Final Shapes?
"In theory, once their constituent amino acids are strung together, proteins attain their final shapes without any energy input. In reality, however, the cytoplasm is a crowded place, filled with many other macromolecules capable of interacting with a partially folded protein. Inappropriate associations with nearby proteins can interfere with proper folding and cause large aggregates of proteins to form in cells. Cells therefore rely on so-called chaperone proteins to prevent these inappropriate associations with unintended folding partners.
Chaperone proteins surround a protein during the folding process, sequestering the protein until folding is complete. For example, in bacteria, multiple molecules of the chaperone GroEL form a hollow chamber around proteins that are in the process of folding. Molecules of a second chaperone, GroES, then form a lid over the chamber. Eukaryotes use different families of chaperone proteins, although they function in similar ways.
Chaperone proteins are abundant in cells. These chaperones use energy from ATP to bind and release polypeptides as they go through the folding process. Chaperones also assist in the refolding of proteins in cells. Folded proteins are actually fragile structures, which can easily denature, or unfold. Although many thousands of bonds hold proteins together, most of the bonds are noncovalent and fairly weak. Even under normal circumstances, a portion of all cellular proteins are unfolded. Increasing body temperature by only a few degrees can significantly increase the rate of unfolding. When this happens, repairing existing proteins using chaperones is much more efficient than synthesizing new ones. Interestingly, cells synthesize additional chaperone proteins in response to "heat shock." "
I wonder of I can get Jano in here to comment on these "Chaperone Proteins", and if they may negate the ability of an Amino Acid chain to be folded incorrectly.
