Answer:
False.
Explanation:
Note that, osmosis is considered as the passive movement of water because,it involves the movement of water from a region or area where concentration is high to the region or area of low concentration. This is the reason why it is compared to or described as a type of diffusion.
This process is known as passive transport or passive movement of water. And it is known to be water specific process.
That is why it can be compared to diffusion of ions or other small molecules in physics.
Answer: Black allele has frequency of 0.14.
Red allele has frequency of 0.86.
The frequency of heterozygotes is 0.241
Explanation: <em>Hardy-Weinberg model </em>states the frequency of alleles in a population will stay in equilibrium as long as there are external influences. It is also used to determine alleles frequencies using the following equations:


p represents frequency of dominant allele;
q represents frequency of recessive allele;
2pq is frequency of heterozygotes;
For the frequency of red allele, which is dominant, we can use:




p = 0.86
For the black allele:



q = 0.14
Frequency of heterozygotes is
2pq = 2(0.86)(0.14)
2pq = 0.241
<u>Frequencies for a population of Muscovy ducks are </u><u>0.86 for red allele, 0.14 for black allele and 0.241 for heterozygote.</u>
There are two types of population growth: exponetial growth and logistic growth
Glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently attached to polypeptide side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated.
In proteins that have segments extending extracellularly, the extracellular segments are also often glycosylated. Glycoproteins are also often important integral membrane proteins, where they play a role in cell–cell interactions. It is important to distinguish endoplasmic reticulum-based glycosylation of the secretory system without of reversible cytosolic/nuclear glycosylation. Glycoprotein of the cytosol and nucleus can be modified through the reversible addition of a single GlcNAc residues that is consider reciprocal to phosphorylation and the functions of these are likely to be additional regulatory mechanism that controls phosphorylation-based signalling.[2] In contrast, classical secretory glycosylation can be structurally essential. For example, inhibition of asparagine-linked, i.e. N-linked, glycosylation can prevent glycoprotein folding and full inhibition can be toxic to an individual cell. In contrast, perturbations of terminal processing, which occurs in the Golgi apparatus, is dispensable for isolated cells(as evidence by survival with glycosides inhibitors) but can lead to human disease (Congenital disorders of glycosylation) and can be lethal in animal models. It is therefore likely that the fine processing of glycans is important for endogeneous functionality, such as cell trafficking, but that this is likely to have been secondary to its role in host-pathogen interactions. A famous example of this latter effect is the ABO blood system.