Helicase breaks hydrogen bonds of the DNA helix. Therefore it “unzips” the DNA helix and separates the strands for free complementary RNA strands which use the strands as a template during replication.
Answer:
In the mRNA sequence AUGGUGCAUGUC the maximum number of amino acids that can be encoded is 4 (option A).
Explanation:
Messenger RNA (mRNA) has a sequence of nitrogenous bases produced by the transcription of a DNA strand. This sequence of bases is organized in triplets or codons —made up of 3 nitrogenous bases— that can encode an amino acid, or mark the beginning or end —STOP codon—of protein synthesis.
From the sequence:
AUGGUGCAUGUC
Four codons are obtained, each of which encodes a different amino acid:
<em>Codons: AUG-GUG-CAU-GUC</em>
<em>Amino acids: Met - Val - His - Val</em>
<em>Methionine Valine Histidina and Valine are the four amino acids encoded by the 12 nucleotide sequence of the mRNA.</em>
Answer:
A. passive transport by diffusion
Explanation:
Diffusion and osmosis are both types of passive transport. They do not require energy. Diffusion is the general term for the process. Osmosis is the diffusion of water molecules.
Many small, uncharged molecules can cross the cell membrane by diffusion. Oxygen and carbon dioxide are examples of two small molecules that pass the cell membrane by passive transport.
Larger or charged molecules require energy to cross the cell membrane. This is achieved by active transport.
Some proteins do indeed need assistance during the folding process. the general term used for the proteins that help other proteins fold is Chaperones.
<h3>What are Chaperones?</h3>
- Chaperones are proteins that help big proteins or macromolecular protein complexes fold or unfold conformationally. There are different groups of molecular chaperones, all of which have the same purpose: to help big proteins fold properly during or after synthesis as well as following partial denaturation.
- Protein translocation for proteolysis involves chaperones as well. The bulk of molecular chaperones aid in protein folding by binding to and stabilizing folding intermediates up until the polypeptide chain is entirely translated, rather than providing any steric information for protein folding.
- Based on their target proteins and location, chaperones have different unique modes of operation.
Learn more about the Protein folding with the help of the given link:
brainly.com/question/28421475
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