The correct answer is option (A) to discover new aspects of the natural world.
The study of rock formations and living organisms in previously unexplored water habitats helps a scientist to discover the newer aspects of the natural world. The unexplored water habitats are the best source to understand the newer aspects of the aquatic bodies like the new species of plants or animals, factors affecting the aquatic life and the different types interactions in the habitats. The study of rock also helps in the study of plants and animals, which were once a part of the habitat, now in the form of fossils.
Thus, the study of rock formations cannot explain the recently observed phenomena as they help in the study of fossils. The study of living organisms in previously unexplored water habitats cannot be applied to test the conclusions of prior investigations and test the predictions of current theories as they remained unexplored.
Answer:
<u>Temperature</u> is most likely the reason of protein unfolding (denaturation).
Explanation:
In the figure attached, coiled (3-dimensional) protein structure is changed to 2 dimensional structure in which protein is unfolded. This is most likely the result of heating proteins which destroys the hydrogen bonds and non-polar hydrophobic interactions that are necessary to establish the tertiary structure of proteins. Principally, increased temperature results in the increased kinetic energy of atoms within a molecule. If the amount of heat is sufficient to break the hydrogen bonds, protein molecule can unfold to 2D structure as shown in the figure.
Answer:
A high level of gene flow into a population tends to be considered to have equivalent allele frequencies and therefore effectively be a single population.
Hope this helps
--Jay
Answer:
Proteins are dynamic entities, and they possess an inherent flexibility that allows them to function through molecular interactions within the cell, among cells and even between organisms. Appreciation of the non-static nature of proteins is emerging, but to describe and incorporate this into an intuitive perception of protein function is challenging. Flexibility is of overwhelming importance for protein function, and the changes in protein structure during interactions with binding partners can be dramatic. The present review addresses protein flexibility, focusing on protein-ligand interactions. The thermodynamics involved are reviewed, and examples of structure-function studies involving experimentally determined flexibility descriptions are presented. While much remains to be understood about protein flexibility, it is clear that it is encoded within their amino acid sequence and should be viewed as an integral part of their structure.
Explanation:
