The correct answer is 50.
Proteins are complex biomolecules made out of amino-acids bound together with peptide bonds. They can be comprised out of thousands of several polypeptide chains with thousands of amino-acids organised in complex structures. But, some of them can contain only around 50 amino-acid and still posses all of the complex traits of an protein.
Some polypeptides contain only 3 amino-acids, but technically they are not classified as proteins due to a big functional and structural differences between a simple polypeptide chain and a protein. Proteins are made out polypeptide chains, but this is only the primary structure of an protein. the polypeptide chains in a protein are organized into complex 3D structures that give them novel traits and complexity as compared to plain polypeptide chains.
Answer:
The correct order is - 3. ribosomes 5. the endoplasmic reticulum 1. the Golgi apparatus. 4. transport vesicles. 2. the plasma membrane.
Explanation:
The protein needs to be transported from the cytoplasm to out of the cells for their target site, for example, insulin and enzymes. The protein synthesizes at the ribosome by the process of translation. It transported to the endoplasmic reticulum and move to the Golgi apparatus where it packaged and modified in the transport vesicles so it can move to, and pass through the plasma membrane.
Thus, the correct order is - 3. ribosomes 5. the endoplasmic reticulum 1. the Golgi apparatus. 4. transport vesicles. 2. the plasma membrane.
The right answer for the question that is being asked and shown above is that: "The <span>variation within the fish population help individuals survive their encounter with the dolphins is that dolphins will tend to be with them and will be served as their own food."</span>
The answer is Denitrification.
Denitrification is the reduction of nitrates back into the largely inert nitrogen gas (N2), completing the nitrogen cycle. This process is performed by bacterial species such as Pseudomonas and Clostridium in anaerobic conditions.
