Because l-glucose is toxic in nature.
Answer:
The appearance of free oxygen in the Earth's atmosphere led to the Great Oxidation Event. This was triggered by cyanobacteria producing oxygen which developed into multicellular forms as early as 2.3 billion years ago
Explanation:
To clarify what I said here are some questions to help!
How did oxygen first appear?
Whiffs in the air is how oxygen first appeared billions of years ago.
For the most part, scientists agree that oxygen, though lacking in the atmosphere, was likely brewing in the oceans as a byproduct of cyanobacterial photosynthesis as early as 3 billion years ago
When was oxygen found?
2.33 billion years ago
Since its first appearance 2.33 billion years ago, oxygen accumulated in high enough concentrations to have a weathering effect on rocks just 10 million years later.
I don't know if this helped you but if it does, please let me know!
Answer:
<u><em>C.)</em></u> <em>Crest to trough</em>
Answer and Explanation:
Protein folding : It is the physical procedure by which a protein chain gains its local 3-dimensional structure, an adaptation that is normally naturally useful, in a quick and reproducible way. It is the physical procedure by which a polypeptide folds into its trademark and useful three-dimensional structure from curl. Every protein exists as an unfurled polypeptide or arbitrary curl when interpreted from a grouping of mRNA to a direct chain of amino acids. This polypeptide does not have any steady (dependable) three-dimensional structure (the left hand side of the primary figure). Amino acids cooperate with one another to create a well-characterized three-dimensional structure, the collapsed protein (the correct hand side of the figure), known as the local state. The subsequent three-dimensional structure is dictated by the amino corrosive grouping.
\The right three-dimensional structure is fundamental to work, albeit a few pieces of practical proteins may remain unfurled, so protein elements is significant. Inability to crease into local structure commonly creates inert proteins, however in certain occurrences misfolded proteins have changed or lethal usefulness. A few neuro degenerative and different ailments are accepted to result from the collection of amyloid fibrils shaped by misfolded proteins. Numerous sensitivities are brought about by off base collapsing of certain proteins, on the grounds that the invulnerable framework doesn't deliver antibodies for certain protein structures.
Answer:
Broad substrate specificity of chymotrypsin would be very dangerous for a protease that plays a role and perform its activities outside of the digestive system.
Explanation:
Chymotrypsin is one of the serine base proteases that includes 3 polypeptide chains. Disulfide bonds held all three polypeptide chains together. Chymotrypsin is a digestive enzyme released by the pancreas into the duodenum.
As a digestive enzyme, chymotrypsin's role is to indiscriminately degrade a large range of proteins that are taken in so that their component AAs can be recovered.
Broad substrate specificity of chymotrypsin would be very dangerous for a protease that plays a role and perform its activities outside of the digestive system.
