Answer:
its c
Explanation:
communicating the result is significant to analyzing data
Answer:
I believe it's A and B
Explanation:
Hope my answer has helped you!
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.
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Answer:
Big leaves cause water loss
Answer:
You are interested in obtaining Staphylococcus aureus for a study investigating the prevalence of methicillin-resistant Staphylococcus aureus in the general population. You have received several samples and are ready to start your isolation procedures. Describe the personal protective equipment that would be needed and three different culturing techniques that can be used to obtain organisms to produce pure cultures. State if you use general or selective media and which specific media you would choose. How would you determine if the culture was contaminated? What is the first step you would take if you detected contamination?
Personal Protective equipment needed; No special precautions are necessary when working with methicillin-resistant staphylococcus aureus, staphylococcus aureus is a bio-safety level
Three different culturing media; to include;
- Etest Method
- Disc Diffusion
- Latex Agglutination.
Properly enriched selective media is used.
The most accurate method for identifying Merthicillin-resistant staphylococcus is to test for the presence of mecA gene by PCR.
The best specific media is latex agglutination test and oxacillin salt agar screen.
How to determine if the culture was contaminated;
It can be spotted by the turbidity of the growth medium or the floating branching mycelia, bacteria contamination can be detected under 10× microscope within few days of contamination.
Step to take if contamination is detected;
Biological contamination is a serious issue and being able to correctly identify different types of contamination is an essential first step in ensuring the safety of your culture.
Explanation:
The literature on methicillin susceptible testing is extensive, and often conflicting in recommendations regarding the most important method for routine use. this is partly because the various studies of phenotypic methods have included different strains, which may differ significantly in heterogeneity and behave differently under particular test condition.
