7. How do weak interactions and disulfide bridges contribute to tertiary protein structure?
Proteins fold into a unique 3D shape in the tertiary structure, based on chemical relationships of the different R groups in the amino acids
Hydrophobic (water repelling) amino acids fold into the centre of the protein
Hydrophilic (water loving) amino acids move to the outside of the protein
Acidic and basic amino acids form salt bridges, stabilizing the protein
Cysteines sometimes form disulfide bridges, also stabilizing the protein
8. What is quaternary protein structure? How does this structure impact function?
Two or more tertiary structure combine to form the quaternary structure of a protein
The final shape here is critical to the proteins function: one wrong amino acid (which can come from a DNA mutation) changes how the protein folds, and thus what it does, if it can still do anything at all. All enzymes, which are critical to proper bodily function, are proteins
9. What are three conditions under which enzymes may be denatured?
A protein denatures when it unfolds and loses its shape
This can result from a change in environmental factors such as temperature, salinity, pH, introduction of a foreign chemical or molecule, among others
10. How do chaperonins assist in the proper folding of proteins?
Chaperonins are small molecules that assist in the folding of proteins
Nobody quite knows how they work, but they can identify unfolded or misfolded proteins and make them fold again
We hope you enjoyed studying this lesson and learned something cool about Proteins! Join our Discord community to get any questions you may have answered and to engage with other students just like you! We promise, it makes studying much more fun 😎
Reece, J. B., & Campbell, N. A. (2011). Campbell biology. Boston: Benjamin Cummings / Pearson.
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