Your going to need show us the experiment, sense all of those are functions there is no question or details for us to answer your question
Answer:
polar bonds
Explanation:
i had the same question on a test of mine and i got it right
Answer:
D. A number of genetically resistant pesticide survivors reproduce. The next generation of insects contains more genes from the survivors than it does from susceptible individuals.
Explanation:
Insect populations already have some insects with pesticide resistance genes. Exposure of insects to pesticides results in the natural selection of these insects with pesticide resistance as they are able to survive and reproduce in the presence of pesticides whereas the other insects die. The resistant insects leave more progeny resulting in the evolution of insect population with increased frequency of pesticide resistance gene.
The correct option is (c) LDL consists of cholesterol and protein.
One of the five main categories of lipoproteins, low-density lipoprotein (LDL), transports cholesterol throughout the body to the areas where it is required for cell repair and deposits it inside the artery walls. They need to be bound to proteins in order to pass through the hydrophilic blood.
The hydrophobic core of the LDL particle is made up of fatty acid esters of cholesterol, while the outer membrane is made up of unesterified cholesterol. The membrane contains a single copy of the hydrophobic apo-B protein, which facilitates the binding of LDL particles to particular cell-surface receptors.
Hence, LDL consists of cholesterol and protein.
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Answer:
The true statement is <em>Hydrophobic side chains are usually in the interior of the native structure</em>.
Explanation:
In the native structure of a protein, the hydrophobic side chains of aminoacids- such as leucine (Leu), alanine (Ala), methionine (Met), and others-are located in the interior of the structure. They are buried inside the structure, whereas polar side chains are exposed to the outside in the structure, and they interact with water molecules.
Regarding the other statements, entropy-as a measure of disorder of a system-is very important in protein stability as we know that native conformations are more ordered systems, with lower entropy and higher stability. Aminoacids in the protein structure interact each other through Van der Waals interactions and hydrogen bonds.
