The observation of the relationships between the anemone and clownfish supports the statement 'symbiotic relationships are important to an ecosystem' it is a fundamental ecological interaction.
<h3>What is symbiosis?</h3>
Symbiosis is a type of ecological interaction where both organisms are benefited from such interaction.
Symbiosis is a fundamental biological interaction that supports the delicate equilibrium (homeostasis) of both marine and terrestrial environments.
The relationships between the anemone and clownfish represent a piece of clear evidence that symbiosis not only helps these species but also the entire ecosystem.
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Answer AND Explanation:
In spite being called the resting phase, many cellular processes take place during this phase. One of the most important of these is chromosomal replication in which each chromosome produces an exact copy of itself. The chromosomes are not visible as discrete structures but instead they appear as diffuse tangle of threads called chromatin.
Another important event is the formation of new organelles like mitochondria. There is also a build up of energy stores which is necessary to drive the mitotic process.
Carbon has four available binding sites and depending on how one atom binds to other atoms, it can form different structures. If you look up the structure of diamond and graphite, you’ll see that they are all made out of carbon but they are arranged differently.
The answer is Have a large surface area on
which chemical enzymes in the digestive system can act on it<span>. This increases the rate of digestion
and absorption of the nutrients. The smaller an object is, the larger the
surface area to volume ration it has compared to relatively larger objects.</span>
Protein structure is the three-dimensional arrangement of atoms in a protein molecule. Proteins are polymers — specifically polypeptides — formed from sequences of amino acids, the monomers of the polymer. A single amino acid monomer may also be called a residue (chemistry) indicating a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond. By convention, a chain under 30 amino acids is often identified as a peptide, rather than a protein.[1] To be able to perform their biological function, proteins fold into one or more specific spatial conformations driven by a number of non-covalent interactions such as hydrogen bonding, ionic interactions, Van der Waals forces, and hydrophobic packing. To understand the functions of proteins at a molecular level, it is often necessary to determine their three-dimensional structure. This is the topic of the scientific field of structural biology, which employs techniques such as X-ray crystallography, NMR spectroscopy, and dual polarisation interferometry to determine the structure of proteins.
Protein structures range in size from tens to several thousand amino acids.[2] By physical size, proteins are classified as nanoparticles, between 1–100 nm. Very large aggregates can be formed from protein subunits. For example, many thousands of actin molecules assemble into a microfilament.
A protein may undergo reversible structural changes in performing its biological function. The alternative structures of the same protein are referred to as different conformational isomers, or simply, conformations, and transitions between them are called conformational changes.
