Answer:
okay so im not a 100 percent sure but i belive it is compare and disscusse the results with other sintist to determin future reserch plans if it is not that then it is publish the result
Explanation:
Answer:
<u>Too much heat can disrupt subcellular structures such as membrane proteins, and enzymes while damaging the integrity of the plasma membrane.</u>
Explanation:
Proteins are macromolecules made up of amino acids. These fold and bond to form several biologically important molecules. For instance, enzymes, a special type of protein functions by <em>providing alternative reaction pathways. They work best at a specific pH and </em><em>optimal temperature range</em><em>, beyond which they become non-functional or denatured entirely. </em>
The denaturing of proteins occur at high temperatures, and alter protein folding, bonding and other types of behavior. Furthermore, membrane proteins are important for regulating cell function. If these are disrupted, the system cannot maintain homeostasis i.e a constant internal environment.
Answer:
Yes, two hydrogen bonds could form between thymine and cytosine.
Explanation:
Cytosine is a pyrimidine base found in both DNA and RNA, and Thymine is a pyrimidine base found in only DNA. Electronegative Oxygen and Nitrogen atoms with free lone pairs are potential hydrogen bond acceptors. Hydrogen atoms attached to very electronegative atoms like Oxygen and Nitrogen have strong partial positive charge and are potential hydrogen bond donors.
One hydrogen bond could form between the C4 carbonyl group on thymine which is a hydrogen bond acceptor and the C4 amino group on cytosine which is a hydrogen bond donor. Also, another hydrogen bond could be formed between N3 of thymine which is a hydrogen bond donor and the N3 of cytosine that is a hydrogen bond acceptor.
It is important to note that hydrogen bond cannot be formed between them because the C2 carbonyl groups found on both bases are both hydrogen bond acceptors.
Plants release oxegen for cellular respiration not carbon dioxide
