In corn plants, the allele for green kernels (G) is dominant over clear kernels (g). A homozygous dominant plant is crossed with a homozygous recessive plant. The parental genotypes are provided for you. Determine the genotype and phenotype of the F1 generation by filling in the Punnett square, then answer the questions by placing the letter of your answer in the answer blank to the right of the question.

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Unit II Assignment—Genetics Worksheet

Solving Punnett Squares

Reginald Punnett was a British geneticist who developed the Punnett square to explain how the chromosomes of parents cross and produce offspring. To solve genetics problems using a Punnett square, it is necessary to a) understand the associated vocabulary and b) understand some of the rules for solving the problems.

• Before you continue with the problems below, review the meaning of the terms allele, dominant, recessive, homozygous, heterozygous, genotype and phenotype.

• You also should review the Punnett Square Basics video linked in the unit lesson.

Instructions: Answer the Punnett square questions below by placing the letter of the correct answer in the blank provided.

The genotypic ratio will be expressed using the alleles given in each scenario (e.g., 50% Gg : 50% gg). The phenotypic ratio will use descriptive terms, e.g., 3 (Green) : 1 (clear), 2 (Green) : 2 (clear), depending on the results of your cross. Be sure not to confuse the two ratios.

Punnett Square Problems

Question 1. In corn plants, the allele for green kernels (G) is dominant over clear kernels (g). A homozygous dominant plant is crossed with a homozygous recessive plant. The parental genotypes are provided for you.

Determine the genotype and phenotype of the F1 generation by filling in the Punnett square, then answer the questions by placing the letter of your answer in the answer blank to the right of the question.

Key: G = green kernels, g = clear kernels

Genotype of parents: _GG_ x _gg_

a) Complete the table below. (4 pts.)

g g
G
G

b) What is the genotypic ratio of the offspring in Question 1? (4 pts.) Answer: ______
a) 50% Gg : 50% gg
b) 100% Gg
c) 25% GG : 50% Gg : 25% gg
d) 100% Green

c) What is the phenotypic ratio of the offspring in Question 1? (4 pts.) Answer: ______

a) 50% Green : 50% Yellow
b) 100% Light Green
c) 25% GG : 50% Gg : 25% gg
d) 100% Green

d) The F1 generation of the cross in Question 1 are all _____. (4 pts.) Answer: ______
a) Homozygous dominant
b) Heterozygous dominant
c) Heterozygous
d) Recessive

 

Question 2: Green seeds are dominant over yellow seeds in pea plants. Cross a heterozygous (green seeded) plant with a yellow seeded plant. The parental genotypes are provided for you.

Determine the genotype and phenotype of the F1 generation by filling in the Punnett square, then answer the questions below.

Key: G = green seeds and g = yellow seeds

Genotype of parents: Gg x gg

a) Complete the table below. (4 pts.)

g g
G
g

b) What is the genotypic ratio of the offspring in Question 2? (4 pts.) Answer: ______
a) 75% Yellow : 25 % Green
b) 75% Gg : 25% gg
c) 50% Gg : 50% gg
d) 35% Green : 65% Yellow

c) What is the phenotypic ratio of the offspring in Question 2? (4 pts.) Answer: ______
a) 75% Yellow : 25 % Green
b) 75% Gg : 25% gg
c) 50% Green : 50% Yellow
d) 35% Green : 65% Yellow

d) The yellow-seeded offspring from the cross in Question 2 are _____ (4 pts.). Answer: _____
a) Homozygous dominant
b) Dominant
c) Homozygous recessive
d) Heterozygous

 

Question 3: Now cross two of the heterozygous F1 offspring from Question 2.

a) Complete the table below. (4 pts.)

G g
G
g

b) What is the genotypic ratio of the offspring in Question 3? (4 pts.) Answer: _______
a) 75% Yellow : 25 % Green
b) 75% Gg : 25% gg
c) 50 Gg : 50% gg
d) 25% GG : 50% Gg : 25% gg

c) What is the phenotypic ratio of the offspring in Question 3? (4 pts.) Answer: _______
a) 75% Green : 25% Yellow
b) 75% Yellow : 25% Green
c) 50% Green : 50% Yellow
d) 100% Green

Question 4: Consider the resulting genotypic ratio of crossing the two heterozygous pea plants in Question 3. We will use this ratio in a short activity exploring probability. Keep in mind crossing two individuals that are heterozygous for a certain trait is similar to flipping two coins. Each coin has two sides (we might think of each side as an “allele”) and the chances of flipping heads/heads, heads/tails, or tails/tails should be similar to the ratio we see when crossing two heterozygotes.

For this simple activity, you will need two coins (pennies, nickels, dimes, quarters, or a mix). Alternatively, you may use Google to find a coin-flipper simulator that will allow you to flip two coins at once. You also will need a piece of scratch paper and a pen or pencil or a blank electronic document.

Directions: Flip the two coins simultaneously at least 50 times. For each flip of the pair of coins, you will record the results on a piece of scratch paper or electronic document. You might set up a table like the one below to record your results. Once you have flipped the coins at least 50 times, enter the number of heads/heads, heads/tails, and tails/tails in Table 1 below, which is part “a” of question 4.

Now determine the ratio for your results. You will do this by dividing the number for each result by the total number of flips, and then multiply by 100. Don’t forget to show your work!

(Example: If the number of heads/heads is 9 then 9/50 = 0.18, 0.18×100 = 18%), Repeat this mathematical procedure for heads/tails and tails/tails); be sure to include your math in the table!

 

a.) Table 1 (12 pts.)
Heads/heads (hh)
Head/tails (ht)
Tails/tails (tt)
Ratio (hh:ht:tt)

b.) Compare the resulting ratio from the Question 3 cross of two heterozygous parents to the ratio from the coin flipping exercise. Are there similarities? If so, what are they? Enter answer in the box below. (4 pts.)

 

 

 

Cancer Risk Factors

5. This question discusses cancer and risk factors. Begin by going to the website http://www.cancer.org/

Click “Cancer A-Z” in the upper-left corner. The page that comes up will provide links to information on breast cancer, colon and rectal cancer, lung cancer, prostate cancer, and skin cancer. Review the information for each these cancers.

Next, write an essay that discusses your own risk factors for each type of cancer and steps you might take to decrease those risk factors. Be sure to address all five types of cancer.

You do not have to disclose any actual personal information if you do not wish to do so. You may create a fictional character and discuss his or her risk factors instead. Be sure to address all five types of cancer.

Your response must be at least 300 words in length, and it must be in your own words. Citations are strongly encouraged. (Type your response below) (40 pts.)

 

Describe your impression of at least one of the speakers in 400-500+ words.

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Reflective Writing

Meet the Experts: Radiology, Naturopathic Medicine, & Emergency Medicine

  • Due Tuesday by 11:59pm
  • Points 0
  • Submitting a text entry box or a file upload
  • Available Jan 9 at 12am – Feb 28 at 11:59pm

Describe your impression of at least one of the speakers in 400-500+ words. Your reflection MUST answer the questions found in the Reflective Writing Rubric to receive full credit.

Review your Learning Assessment 2 and identify the questions you answered incorrectly. Using the textbook linked in blackboard locate the correct answers to all your missed questions.

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Intro to biology

 Learning Assessments 2 Corrections Assignment .docx

1. Review your Learning Assessment 2 and identify the questions you answered incorrectly.
2. Using the textbook linked in blackboard locate the correct answers to all your missed questions.
3. Provide an explanation (in complete sentences) of why the newly chosen answer is correct.
4. You may skip all questions you answered correctly on Learning Assessment 2.

How many monomers (also called subunits) are in this protein? Are they similar in shape or dissimilar? How many individual polypeptide chains are in this protein?

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Protein Folding

Part I:  Protein Folding

The shiga-like toxin (ST) is a protein-based toxin produced by the bacterium Enterohemorrhagic Escherichia coli (EHEC), which is the causative agent responsible for most cases of bloody diarrhea.  Believe it or not, much of the disease symptoms associated with EHEC infection derives from the cytotoxic effects of ST, whose protein ribbon structure is shown below.  Analyze these images (both the side and bottom view) and answer the following questions:

Side View                                                                           Bottom View

 

  1. (2 points) How many monomers (also called subunits) are in this protein?  Are they similar in shape or dissimilar?
  2. (2 points) How many individual polypeptide chains are in this protein?
  3. (2 points) How many unique polypeptide chains do you think are in this protein?
  4. (2 points) What type of structure is shown here (1o, 2o, 3o or 4o)?
  5. (2 points) What would be a good descriptive (but scientific) classification for this protein?  Hint:  Consider our description of hemoglobin as it pertains to the nature and number of subunits contained therein.
  6. (3 points) Identify two different forms of secondary structure in this protein (use arrows and label them appropriately).  If one type of secondary structure is not present, indicate so in your answer below.

Part II:  Enzymatic Active Site Motifs

Below is an image of an enzymatic active site, which is occupied by the enzyme’s substrate (shown below, left).  This enzyme catalyzes the reaction that changes cyclic AMP (shown in the active site) to AMP.

 

Cyclic CMP

 

  1. (3 points) Explain why this enzyme cannot bind to cyclic CMP and catalyze the reaction that would change cyclic CMP (shown above, right) to CMP.  Please be specific in your answer.
  2. (3 points) What would happen to the enzyme’s affinity for cyclic AMP if the enzyme’s active site had a missense mutation that changed the Threonine residue (blue) to Valine?  Briefly explain your answer.
  3. (3 points) What would happen to the enzyme’s affinity for cyclic AMP if the enzyme’s active site had a missense mutation that changed the Serine residues (orange and dark green) to Threonine?  Briefly explain your answer.
  4. (3 points) Take a closer look at the active site for this enzyme and examine the noncovalent interaction mediated by the residue highlighted in pink.  Is it possible for a mutation to alter this residue in such a way as to eliminate this noncovalent interaction with cyclic AMP?  Briefly explain your answer.

 

Part III:  Multimerization

Protein families arise when a protein sequence that generates a stable fold diverges over many generations and acquires new functions.  One example of this can be seen in the globin family.  Myoglobin (shown below, left) is a stable monomeric protein that can help carry oxygen using a heme molecule (cofactor).  On the other hand, hemoglobin (shown below, right) is only functional as a tetramer and while it also uses heme to carry oxygen, it is useful over a much more dynamic range than myoglobin.  The “globin fold” is structurally conserved across these proteins, but the ability to tetramerize arose through genetic drift and natural selection.

  1. (5 points) Thinking back about what we learned about DNA sequence mutations and their effect on protein structure, provide an explanation for how changes in the polypeptide sequence of these two proteins can still produce the same overall fold (i.e. alterations that conserve protein structure) but have slight differences in the protein’s ability to multimerize (i.e. alterations that alter protein-protein interactions).
  • Another way to think about this is to consider what kind of mutations might promote multimerization (polar vs. nonpolar) in an aqueous environment and where would you expect these changes to be within the overall protein structure (surface vs. core)?

 

 

BONUS (1 point):  Considering their structure (and what you know about synthesizing polypeptide chains), hypothesize why proline residues are often positioned at sharp turns in the polypeptide sequence.  Why might that be the case?  Hint:  try drawing a tripeptide chain where proline is the second residue.

 

Briefly summarize the data shown in the figure. Be sure to compare the phenotypes from the bacterial strains where the GOI was deleted vs. the bacterial strains where individual amino acid substitutions were introduced into the GOI.

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Biochemical Pathways

Below are representative transmission electron micrographs (TEM) of the WT and mutant P. gingivalis strains as well as quantitative data that measures the quantity of OMVs produced by these bacterial strains.  To generate the graph, please note that the Alaei lab used a fluorescent probe to quantitate the relative levels of OMVs produced by the WT or mutant P. gingivalis strains.  Use this data to answer the following questions.

 

1. (2 points) Briefly summarize the data shown in the figure.  Be sure to compare the phenotypes from the bacterial strains where the GOI was deleted vs. the bacterial strains where individual amino acid substitutions were introduced into the GOI.

 

2. (2 points) Provide a hypothesis that could have been tested using this experiment.  Your hypothesis should include a potential function for the protein encoded by the GOI.  In other words, how might this gene be involved in OMV production?

 

3. Let’s consider the possibility that GOI encodes a phosphatase. Recall that phosphatases are enzymes that dephosphorylate proteins or other biomolecules.  For the sake of simplicity, assume that this phosphatase catalyzed half of the reaction shown below (i.e. the enzyme removed one of the phosphate groups on the molecule shown on the left):  2H2O ++ 2HPO42-

  • (3 points) Given that the GOI product is a phosphatase, would you assume that the reaction shown above is exergonic or endergonic?  Explain your reasoning.
  • (3 points) Porphyromonas gingivalis lives exclusively in mammalian hosts.  Would you expect the phosphatase encoded by GOI to be active at -20oC?  How about 150oC?  Explain your reasoning.
  • (3 points) Given their phenotypes, did the single amino acid substitutions (R88A, H116A and H157A) alter the catalytic activity of this phosphatase?  What level(s) of protein structure (primary, secondary, tertiary, quaternary) would you expect to be altered by mutations that impact phosphatase activity?  Briefly explain your answer.
  • (3 points) Based on what you know about enzymes (and the phenotypes associated with the mutant gingivalis strains), where in the protein might the amino acid substitutions be located?  Why would altering protein structure at this site result in the phenotypes that you see illustrated in the figure?

Hint: what is a common structural feature of enzymes that facilitates their role in catalyzing chemical reactions?

 

4. (4 points) Do the single amino acid substitution (R88A, H116A and H157A) mutants display the same phenotype as the null mutant strain (i.e. the mutant strain where the GOI was deleted)?  What about genotypes (are they the same or different)?  Briefly explain your answer.

 

5. (4 points) If Dr. Alaei’s research group had already discovered that deleting the GOI caused the phenotype shown above, why would they want to study the single amino acid substitution mutants?  What would this add to our understanding of the mechanism driving OMV formation.

 

6. (4 points) Consider the specific amino acids that were mutated in the gingivalis mutants (R8A, H116A and H157A).  Describe the nature of the mutations (how do the R-groups of substituted amino acids differ from the amino acids that they replaced) and predict whether these specific mutations are likely to have impacted the primary, secondary, tertiary and/or quaternary structure of the phosphatase encoded by the GOI.  Explain your reasoning.

 

7. (2 points) What type of point mutations do you think underlie the amino acid substitutions in the GOI (conservative/nonconservative missense, nonsense, silent, frameshift)?  Explain your reasoning.

 

BONUS (1 point):  The substrate of the phosphatase encoded by the GOI is not a protein (see Q#3).  What larger macromolecule or cell structure might that molecule be a part of and how could modulating its phosphorylation level modulate budding of vesicles off the bacterial cell surface?

 

The Krebs cycle adds a 2-carbon molecule to a 4-carbon molecule to produce a 6-carbon molecule. If we wanted to create an alternative cycle that uses 10-carbon input molecules, what could the rest of the Krebs cycle intermediates be?

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Lab 7:  Understanding Cellular Respiration

 LAB GOALS:

  • To understand the logic of the process of cellular respiration.
  • To conquer the fear and loathing of navigating these biochemical processes & pathways!

 OUTLINE:

  1. Overview and Introduction
  2. Glycolysis
  3. Krebs Cycle
  4. Electron Transport and Oxidative Phosphorylation
  5. Putting it all together!

INTRODUCTION:

Today we are going to use simple problem-solving techniques to figure out how our cells can dismantle the glucose molecule to provide energy in the form of ATP.  Although it can look daunting at first, these processes actually follow a logical progression that can be deciphered without too much agony.

STOW AWAY ALL YOUR NOTES & DEVICES!  USE LOGIC ONLY FOR THIS ACTIVITY!

 

PART 1:  Glycolysis

Obtain a GLYCOLYSIS packet for your group.  This packet should contain:

  • 9 Green Cards
  • 4 Yellow ATP Cards
  • 1 Yellow NAD Card

(It’s a good idea to check before you start that you have all the necessary cards.)

On the mitochondrion mat, order the green cards to show the 9 steps of glycolysis.  This is a problem-solving exercise, not a memorization test.  You should be able to order the green cards without any prior knowledge of glycolysis solely by elimination and chemistry logic.  The final solution will make sense with the arrows on the laminated map.  You can start adding the yellow cards where they make sense.

NOTE:  Biological chemistry is driven by carbon and phosphate.  If you try to keep track of hydrogen or oxygen, these reactions will drive you crazy!  Why?  Because we are working in an aqueous environment and parts of water molecules are enveloping all the reactants almost all of the time.  Focus on carbon!

When you arrive at a Glycolysis pathway that you think is correct, ask your instructor to check your progress.  If you have not yet arrived at the correct pathway order, keep working until you do!  When you arrive at a correct pathway, do a ‘speed round’ by mixing up the cards and trying to recreate the correct solution as quickly as possible.  Less than 20 seconds is good.  (The reason we do this is not to encourage speed-memorization, but to practice logic at high speeds, which is a different method for challenging our brain to make sense of a complicated pathway).

When you have finished, discuss the following questions briefly with your group.  Answers are located on the last page of this guide.

 

Glycolysis Discussion Questions:

  1. In step 3, there is an arrow between reactant and product. Does this arrow signify an enzyme?
  2. There are two ATP-spending cards in this process, and two ATP-creating cards. Is this process ‘ATP neutral’?
  3. [A really hard thought question] Which of the enzymes in Glycolysis do you think evolved earliest?

 

After you have finished with the Glycolysis packet, replace all of the cards in the packet and exchange it for a Linking Step & Krebs Cycle Packet.

 

 

PART 2:  Arranging the Krebs Cycle and Linking Step

Check to make sure your Linking Step & Krebs Cycle Packet contains:

  • 12 Red cards of varying sizes
  • 6 Yellow cards (1 ATP, 4 NADH and 1 FADH2)

Now that you’ve practiced some problem-solving with the Glycolysis Packet, you are ready for an even more difficult challenge.  Starting with pyruvate (which you might recognize as the 3-carbon molecule that was the end result of glycolysis) you should attempt to place the cards in order through the Linking Step and the Krebs Cycle.

You’ll need to create a Krebs Cycle that can be repeatedly loaded with input molecules.  Notice that there is a circular pathway that is ‘fed’ by the linking step.  The molecules you chose to be the reactants in the step that starts this circular pathway need to correspond to the larger molecule that starts the cycle.  In other words, what you put in should correctly start the series of reactions.  When you find the correct solution, this will make sense.

At some points in this cycle, redox reactions will take place.  Occasionally, we need to determine whether a redox reaction has occurred between organic molecules that have the same number of carbons.  We have a specific algorithm for this:

  1. Count the C-H bonds in the reactant.
  2. Count the C-C bonds in the reactant.  Double bonds count as 2 C-C bonds.
  3. Add these numbers together to get the ‘Reactant High Energy Bond Number.’
  4. Count the C-H bonds in the product.
  5. Count the C-C bonds in the product.  Double bonds count as 2 C-C bonds.
  6. Add these numbers together to get the ‘Product High Energy Bond Number.’
  7. If the Reactant High Energy Bond Number does not equal the Product High Energy Bond Number, then a redox reaction has occurred.

Does this algorithm make sense to you?  This is a formal way of deciding whether the energy state of a molecule has changed simply by counting the bonds that tend to have more energy in them (C-C and C-H).  You may need this algorithm to determine where to place certain yellow cards in this packet.

NOTE:  The electron-carriers FADH2 and NADH can be tricky.  Each carries a hydrogen and 2 electrons.  Each is reduced to their energy-carrying form by oxidizing carbon.  The energy levels of these two carriers are slightly different (as we will see in the Electron Transport Chain).  However, there is no logical reason that you should be able to determine which redox step is FADH2 rather than NADH.  Your instructor will help you with this detail.  This is due simply to a difference in the enzyme used to catalyze that step.

Use of the lower-output FADH2 may be a way to protect against poisons or mutations that might damage NADH usage (an internal redundant system).  It may also be vestigial; we may simply be in the process of evolving towards use only of higher-energy NADH and this is the last enzyme that has yet to make the evolutionary switchover.  Like many evolutionary questions, we don’t know for sure (and the scope of this question is a bit beyond this class).

CoA-containing intermediates have a high-energy S-C bond.  In one place, this high-energy bond is used to create an important C-C bond.  In another place, CoA-C energy is released in a catalyzed reaction that produces GTP.  GTP is of similar energy to ATP, and is converted quickly to that more common energy currency.

When you arrive at a Krebs Cycle that you think is correct, ask your instructor to check your progress.  If you have not yet arrived at the correct pathway order, keep working until you do!  When you arrive at a correct pathway, do a ‘speed round’ with the Krebs Cycle.  Less than 25 seconds is good.

When you have finished, discuss the following questions briefly with your group.  Answers are located on the last page of this guide.

 

Linking Step and Krebs Cycle Discussion Questions:

  1. Give a one-sentence basic summary of the purpose of the Krebs Cycle.
  2. The Krebs cycle adds a 2-carbon molecule to a 4-carbon molecule to produce a 6-carbon molecule. If we wanted to create an alternative cycle that uses 10-carbon input molecules, what could the rest of the Krebs cycle intermediates be?  (There are many possible answers.)
  3. What is the major difference in the linking step between prokaryotes and eukaryotes? In which type of cell is the linking step probably more difficult to carry out?

After you have finished with the Linking Step & Krebs Cycle Packet, replace all the cards and exchange it for an Electron Transport & Oxidative Phosphorylation Packet.

 

 

PART 3:  Re-Enacting the Electron Transport Chain

Make sure your Electron Transport & Oxidative Phosphorylation Packet contains:

  • 8 Blue or Purple cards of varying sizes
  • 3 Yellow Cards
  • A handful of small H+ and e- cards

You’ve already recreated the processes that have led to the production of reducing equivalents in the form of NADH and FADH2.  In this third packet, you’ll demonstrate the use of those electrons to produce a proton gradient which will be used to create ATP.

Begin by placing the complexes in the mitochondrial membrane of your laminated eukaryotic cell.  NADH drops off two electrons and a proton at Complex I, while FADH2 electrons and protons are added to Complex II.  Both Complex I and II can then transfer electrons to a slightly lower energy state on Coenzyme Q.  Electrons move from higher energy states to lower energy states from this mobile protein Q to Complex III to mobile protein Cytochrome C to Complex IV.  At Complex IV, electrons are transferred to the extremely low energy electron acceptor O2.

During this process, the energy of the electrons is used to transport protons to the inner mitochondrial membrane at Complexes I, III and IV.

NOTE:  In prokaryotes, this process occurs in the cellular membrane.  While essentially the same, the key difference is that prokaryotes are pumping protons into the outer environment, ending up with a net gradient inside the cell that is relatively low in protons, pulling protons back into the cell through ATP Synthase.

Demonstrate the flows of electrons, protons and the changing ATP/ADP molecules as the process continues first for NADH, and then repeat the demonstration for FADH2.  You should be able to watch the membrane gradient build up and then recover.  All group members should feel comfortable leading this demonstration and talking through the process.  When you feel comfortable with your understanding of this process, demonstrate it for your instructor with input from all group members.  When your instructor is confident in your understanding, move on to the following discussion questions.

Electron Transport & Oxidative Phosphorylation Discussion Questions:

  1. Why are electrons delivered via NADH more valuable than those delivered to the ETC via FADH2?
  2. What is the role of oxygen in cellular respiration?
  3. How are the ETC complexes arranged in the inner mitochondrial membrane?

After you have finished with the Electron Transport & Oxidative Phosphorylation Packet, replace all the cards and put it back in the piles with the other packets.

 

Are gender traits completely a result of societal expectations? Are there any parts of the human body that get oxygen directly from the air and not from the blood? Are there nuclear reactions going on in our bodies?

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Cell respiratory

JO, Biology

  • Are gender traits completely a result of societal expectations?
  • Are there any parts of the human body that get oxygen directly from the air and not from the blood?
  • Are there nuclear reactions going on in our bodies?
  • Can humans ever directly see a photon?
  • Can I turn my cat into a diamond?
  • Do blind people dream in visual images?
  • Do Kirlian photographs show the soul of an organism?
  • Do koalas eat honey like other bears?
  • Do poppy seeds contain narcotics?
  • Does the human body contain minerals?
  • How can the heart be strong enough to pump blood up your legs against gravity?
  • How can we differentiate so many different foods if we can only taste four flavors on our tongue: sweet, bitter, sour, and salty?
  • How can we unlock the 90% of our brain that we never use?

What skills and knowledge related to the course topics do you currently have? What do you want to learn during this course? How will you determine whether this course has been successful for you?

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Answer this questions about epidemiology , not more than 300 words

Part 1:
Current skills:
What skills and knowledge related to the course topics do you currently have?

Want to Learn:
What do you want to learn during this course?

Your success:
How will you determine whether this course has been successful for you?

List the characteristics that unite all animals. List the characteristics that are used to classify and divide the animal phyla. Observe the diagram below that represents a Marine Biome.

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Pre-Lab Questions

  1. List the characteristics that unite all animals.
  2. List the characteristics that are used to classify and divide the animal phyla.
  3. Observe the diagram below that represents a Marine Biome. (Drawing by Dr. Palavecino- not to scale)

 

What was the article about? Which methods were used in the article? What are the major finding of the article? Explain in no more than 3 sentences how the information in the article points to the designing work of a Creator.

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Week 6 Reflection

Instructions: Read the Week 6 Article posted on Blackboard.

 Write your responses below in the green boxes.

NOTE: The green boxes will expand when you type to the end of them.

  1. Purpose of the Research. What was the article about? This is a brief response—no more than 5 sentences total
  2. Methods. Which methods were used in the article?
  3. What are the major finding of the article?
  4. Explain in no more than 3 sentences how the information in the article points to the designing work of a Creator.

Now Submit this completed Document to Blackboard to be graded.