Answer:
Because each subject in an experiment has to have equal conditions to ensure the most accurate results. And water temperature is known to impact plant growth. An experiment using different water temperatures is a terribly inaccurate experiment.
Answer:
True.
Explanation:
<em>"adjective
</em>
<em>adjective: intermediate
</em>
<em>coming between two things in time, place, order, character, etc."</em>
Pictures correlating to the crime scene are like puzzles to find out the other meanings or cause of another picture.
For example:
A opened jug of milk sits on a table.
There's a blurred figure of a hand hitting the jug.
The jug is now laying on the table, dripping everywhere.
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If we take out the middle picture "There's a blurred figure of a hand hitting the jug.", then we would not know what hit it over. Did someone bump into the table? Did a cat climb onto the table and release its almighty strength onto it? All we would know that it was once standing upright.
TLDR; Without intermediate pictures, it would be hard to grasp what happened on the scene. Intermediate pictures all have something in common with each other to help interpret what occurred to the viewer.
Answer:
C. The differences between the observed and expected counts are too large to be attributed to chance.
Explanation:
The p-value of the statistic represents the chance that the observed count is based on luck or chance. When p value too high, the research can't be used since the chance that its not represent real condition are too high. Most researchers use 5% (0.05) as the cutoff of something called statistically significant. In this research, the p-value is 0.04 or 4%, so it is statistically significant.
Tertiary Structure<span> - refers to the comprehensive 3-D structure of the polypeptide chain of a </span>protein<span>. There are several types of bonds and forces that hold a protein in its tertiary structure. </span>Hydrophobic interactions<span> greatly contribute to the folding and shaping of a protein. The "R" group of the amino acid is either hydrophobic or hydrophilic. The amino acids with hydrophilic "R" groups will seek contact with their aqueous environment, while amino acids with hydrophobic "R" groups will seek to avoid water and position themselves towards the center of the protein. </span>Hydrogen bonding<span> in the polypeptide chain and between amino acid "R" groups helps to stabilize protein structure by holding the protein in the shape established by the hydrophobic interactions. Due to protein folding, </span>ionic bonding<span> can occur between the positively and negatively charged "R" groups that come in close contact with one another. Folding can also result in covalent bonding between the "R" groups of cysteine amino acids. This type of bonding forms what is called a </span>disulfide bridge<span>. </span>Primary Structure - describes the unique order in which amino acids are linked together to form a protein. Proteins are constructed from a set of 20 amino acids. <span>All amino acids have the alpha carbon bonded to a hydrogen atom, carboxyl group, and amino group. The </span>"R" group<span> varies among </span>amino acids<span> and determines the differences between these protein monomers. The amino acid sequence of a protein is determined by the information found in the cellular</span>genetic code<span>. The order of amino acids in a polypeptide chain is unique and specific to a particular protein. Altering a single amino acid causes a </span>gene mutation, which most often results in a non-functioning protein.
<span>Secondary Structure - refers to the coiling or folding of a polypeptide chain that gives the protein its 3-D shape. There are two types of secondary structures observed in proteins. One type is the alpha (α) helix structure. This structure resembles a coiled spring and is secured by hydrogen bonding in the polypeptide chain. The second type of secondary structure in proteins is the beta (β) pleated sheet. This structure appears to be folded or pleated and is held together by hydrogen bonding between polypeptide units of the folded chain that lie adjacent to one another.
</span><span>Quaternary Structure - refers to the structure of a protein macromolecule formed by interactions between multiple polypeptide chains. Each polypeptide chain is referred to as a subunit. Proteins with quaternary structure may consist of more than one of the same type of protein subunit. They may also be composed of different subunits. Hemoglobin is an example of a protein with quaternary structure. Hemoglobin, found in the blood, is an iron-containing protein that binds oxygen molecules. It contains four subunits: two alpha subunits and two beta subunits.
I hope this helped you find the answer you were looking for!
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Correct answer: D) From bacteria living in their roots
Nitrogen is an essential plant nutrients, but it is metabolically unavailable to higher plants and animals. It is available to some species of microorganism by biological nitrogen fixation in which nitrogen is converted to ammonia with the help of enzyme dinitrogenase.
The process of breaking apart the two atoms in a nitrogen molecule is called nitrogen fixation. Plant obtain the nitrogen they need from the soil which is already fixed by the bacteria and archae.
Example: <em>Azobacter</em><em>,</em> Nostac
