Scientific Research Paper Guidelines
You will conduct an individual research experiment, and a few weeks later, write and turn in a
scientific research paper reporting on your experiment. A sample paper is given for you at the
end of these instructions. The report should convey your complete understanding of the research
that you conducted. It should be written primarily in past tense. First person should be
avoided. It should be 4-5 pages, typed, double-spaced, and include the following sections,
labeled, in this order:
1. Title Page of the report, your name, date, course name, and the name of the instructor should
be on the cover page. The title should be specific. For example: The effects of light
and dark on seed germination. NOT: Seed Germination.
2. Abstract:
The abstract is a short passage (a paragraph) that summarizes the major points of the
paper: objectives, methods, results, and conclusions. It may be easiest to write the
abstract last, although it comes first in your paper. It must be informative but brief and to
the point.
3. Introduction:
The introduction should include background information, the purpose of your
experiment, and an explicit statement of the hypothesis. Give relevant background
information
and an overview of your topic. State the objective or purpose of your experiment. End
your introduction with a clear statement of your hypothesis (eg.: It was hypothesized that
the population size of snails would be inversly related to distance from shoreline.). Use
references to find background information and cite these references in the text at the end
of the sentence or paragraph (see below). You must directly acknowledge the source
of any material, ideas, or concepts that are not your own!! The failure to do so is
plagiarism!! If you use the author’s direct words, you must enclose his words in quotes
(“) and include a citation. However, direct quotes should be avoided. Paraphrase the
author’s ideas in your own words, and cite the reference at the end of your sentence.
Citations should follow one of the appropriate formats shown below or see
www.mla.org/style/sources.
4. Materials and Methods:
This section of your report tells the reader how the experiment was conducted, what
equipment was used, and how data was collected, with enough detail that he/she could
repeat it if they wanted to (recall the importance of repeatability to the Scientific
Method). It should be written in complete sentences and paragraphs, NOT lists, and in
past tense. It should identify the variables for the experiment, what measurements
were made, how measurements were made, and what controls were used.
5. Results:
The results section of the paper should summarize and illustrate your data
(measurements and observations). It should be well organized and present the data in a
logical order. You should include all of your data in tables or figures which are properly
labeled, and also describe these results in a few paragraphs, referring back to the tables
and figures (DO NOT interpret data in this section, just present your findings,
interpretation belongs in the next section). A table or figure by itself does NOT
constitute a results section. Remember to include all parts of a table or figure, including a
title, labels, and a legend.
6. Discussion and Conclusions:
The discussion should explain and interpret the results: i.e. tell the reader why you
think you got the results you got and what the results mean. For example, do the data
support your hypothesis? How or how not? (Remember, one experiment does NOT
“prove” a hypothesis!) You may refer back to your data as evidence to support your
conclusions. Also, explain why you think you got the results you did. Address the
question of how your results are relevant to the topic of the experiment, i.e. the “big
picture”. How can the results be applied? Use references to find other similar
experiments that have been conducted and cite these references in the text (see below).
Discuss how your results differ or are similar to these other experiments. Also, discuss
any possible sources of error in your experiment and any future research that would be
helpful.
7. Literature Cited:
The literature cited is like a bibliography, but it lists only those sources which you have
actually cited in your text. This should be the last page(s) of the report. Arrange your
references alphabetically by each author’s last name, and indent under the first line.
Leave 2 spaces between listings. Your report must cite at least three references, which
may include your textbook. Encyclopedias and dictionaries are not acceptable
references.
Citing References in the text:
Generally, use the author’s last name and the year of publication.
for a work by one author:
…“sexual dimorphism in the species” (Jackson, 1976).
for a work by two authors:
… found to be of the heterozygous type (Jackson and Ard, 1988).
for a work by multiple authors:
… entirely due to the independent variable (Jackson, et al. 1982).
for an author whose name is used in the sentence:
… Jackson found similar results with his mice (1990).
for a web page or reference without a specific author, use the title and year:
… genetically altered mice that glow (Mice Genetics, 2001).
Listing References in the Literature Cited:
List the author first (by last name), then the year, the title, and publication information.
for a book:
Jones, C. W. and W. D. Billings. 1992. The Genetics of Fruit Flies. 2nd ed.
Wadsworth Publishing Company, New York.
for an article or chapter in an edited book:
Jackson, T. 1990. The effects of pH changes on saltwater aquaria. Pages 23-31
in H. H. Hobbs, ed. The Complete Aquarium. Yale University Press, New
Haven. (NOTE: Hobbs is the editor, Jackson is the author.)
for an article in a journal or magazine:
Jenson, A. B. 1994. The diffusion of potassium permanganate molecules in water.
Science 70:457-459. (NOTE: Science is the name of the journal, 70 is the
volume #, 457-459 are the pages on which the article was found.)
for a personal web page:
Lancashire, Ian. 1997. Genetics.
http://www.chass/utoronto.ca:8080/ian/index.html, accessed Nov. 11,
2004.
for a professional web site without a specific author:
The Human Genome Project Information. n.d.
http://www.ornl.gov/TechResources/HumanGenome/home.html, accessed
Nov. 11, 2004.
Some helpful hints of writing:
1. Make an outline. Outlines help to organize your thoughts and will limit redundancies.
2. Write simply and concisely. Say what you mean and avoid catchy phrases. This is not creative
writing.
3. Avoid starting sentences with: However, Therefore, Also, Yet, Then, And, Or, In my
opinion, I believe, I think, I feel, It also. Other words to avoid: thing, also, it, I believe,
surely, very.
4. Transition: Be sure to transition from paragraph to paragraph. This is not a grocery list.
Some common problems:
Too casual
Say for instance, a famous movie star wanted to be cloned, ok that’s cool but, what happens…
Too vague
I believe the human genome project will bring hope to the economic and medical future.
Exaggerated statement
This is a project studied by not only the United States, but by all, other countries, it is an
international project.
Run-on sentence – break items up into separate sentences or use commas.
Surely this information will become valuable by scientist selling this information or trying to
make money instead of helping people this technology will be abused.
Consistent verb tense
This worldwide research effort had the goal to analyze the human structure of the DNA and
knowing the location of one hundred thousand human genes.
Redundancy
Basically that’s how the human genome project works and hopefully later in the future we
will have…
SAMPLE PAPER
The Effects of Temperature on the
Horseradish Peroxidase Enzyme.
Name
Date
Course
ABSTRACT
Temperature is known to be an important factor in enzyme activity. In this study, the effect of
different temperatures on the activity of the enzyme peroxidase was determined using the
substrate guaiacol. A color change of the enzyme reacting with guaiacol was measured using a
spectrophotometer. The enzyme was subjected to four different temperatures: 250C, 350C, 450C
and 550C. Absorbance readings of the reaction were measured in the spectrophotometer over a
period of time of 60 seconds for each temperature. The different temperatures did have an effect
on the enzyme’s activity. The absorbance readings for 250C, 350C, and 450C were all very
similar, however, the reaction at 350C had the greatest rate of activity. The reaction at 550C had
the lowest rate of reaction. This shows that the optimal temperature for the enzyme peroxidase is
350C.
INTRODUCTION
Enzymes are protein molecules that function as biological catalysts. They enable cells to
perform a multitude of chemical reactions very rapidly by lowering the energy of activation
required to initiate the reaction. In this process of speeding up the reactions, the enzymes are not
used up or chemically altered. They can be used over and over again in the cell. The enzyme
works by binding with the substrate, and then changing shape to cause the reaction to occur with
less energy and produce the product (Campbell et al. 1999).
An enzyme’s environment can affect the activity of the enzyme. Temperature, pH,
substrate concentration, and enzyme concentration can all influence the activity of an enzyme.
Since enzymes are proteins, their secondary and tertiary structure is important in their function.
If the hydrogen bonds that determine this structure are destroyed, the enzyme will denature, or
lose its shape, and no longer function. Denaturation can be caused by extreme temperature or
pH (Campbell et al 1999).
Substrate and enzyme concentration can also influence enzyme activity. Enzyme activity
will generally be higher with higher substrate concentration, until the enzyme becomes saturated
(all of the enzyme molecules are being used). Then, to increase activity, the enzyme
concentration must be increased (Floyd 2001).
Enzyme activity can be determined by measuring the amount of product that is produced.
If the product of the reaction is a different color than the substrate, then this color change can be
measured in a spectrophotometer. This device measured the amount of light that is absorbed by
a solution. The darker the color of the solution, the more light will be absorbed. The reaction
mixture can be placed in the spectrophotometer and the absorbance recorded as the reaction
occurs.
The enzyme peroxidase can be easily derived from horseradish. Peroxidase in the
presence of hydrogen peroxide reacts with the substrate guaiacol. Guaiacol can be derived from
the resin of a tree. The reaction of guaiacol with peroxidase causes a color change from reddishbrown to clear. This color change can be monitored in a spectrophotometer to observe the rate of
reaction (Floyd 1999).
To find the optimal temperature conditions for peroxidase, the enzyme was subjected to
four different temperatures. It was hypothesized that room temperature, 250C, would produce
the greatest enzyme activity, and therefore the greatest color change as measured by absorbance
in the spectrophotometer.
MATERIALS AND METHOD
Four test tubes were prepared with 1 mL of substrate (5mM guaiacol and 2% hydrogen
peroxide) and 1mL of buffer (citric acid-disodium phosphate at pH6). One test tube was kept at
room temperature (approximately 250C). The other three test tubes were placed in three separate
water baths (350C, 450C and 550C) and allowed twenty minutes to equilibrate. The
spectrophotometer was blanked at 470nm with the room temperature test tube of substrate and
buffer. Then, 0.l mL of enzyme (lxl0 M peroxidase) was measured with a pipette and quickly
added to the room temperature test tube and it was immediately placed into the
spectrophotometer. The readings from the spectrophotometer were recorded in five-second
intervals for a period of one minute. The procedure was repeated for the other 3 test tubes. The
absorbance readings were then graphed.
RESULTS
The test tube at 250C had the highest final absorbance of 0.123 (see Figure 1). This
reaction also had the most change over the one minute period, from 0.039 to 0.123, however the
initial rate of change was 0.00165 nm/sec. The test tube at 350C had a final absorbance of 0.115
and a total change of 0.097. This reaction had the greatest initial rate of change 0.0018 nm/sec.
The 450C test tube reached a final absorbance of 0.099 and had a total change of 0.047, but the
initial rate of change was 0.0017 nm/sec. The 550C test tube had a final absorbance of 0.052 and
a total change of 0.008. The initial rate of change was 0.00087 nm/sec.
Figure 1. The absorbance readings of peroxidase at different temperatures.
0.14
Absorbance 470
0.12
0.1
25 C
0.08
35 C
0.06
45 C
0.04
55 C
0.02
0
0
5
10
15
20
25
30
35
40
45
50
55
60
65
Time (seconds)
DISCUSSION AND CONCLUSIONS
This experiment shows that temperature does have a significant influence on the activity
of enzymes. The results for 250C, 350C, and 450C were all very similar, however, the reaction at
350C had a slightly greater rate of activity. This indicates that 350C is the optimal temperature
for the horseradish peroxidase enzyme, contrary to the original hypothesis. This indicates that
horseradish should be stored in cool temperatures to prevent breakdown. The test tube at 550C
showed the least amount of activity. At this temperature, the enzyme must have begun to
denture and no longer be able to function.
An experiment using soybean peroxidase (SBP) found the SBP to still function at 900C.
The article states that SBP is substantially more thermostable than horseradish peroxidase
(McEldoon and Dordick 1996). Another experiment using peroxidase purified from rice hulls
found that it is also stable at higher temperatures (Ryu and Kim 1997). Human enzymes usually
have an optimal temperature of approximately 350C to 400C, close to human body temperature
(Campbell, et al. 1999). However, horseradish peroxidase is not a human enzyme, nor is it
soybean peroxidase. This experiment shows that the optimal temperature for horseradish
peroxidase is 350C and that its function begins to deteriorate at temperatures of 550C.
Although this experiment was performed very carefully, there are two major sources of
error which may have affected the results. The enzyme may not have been measured accurately
in the test tubes. The small amount of enzyme used, 0.1 mL, was difficult to measure by hand
pipetting. An automatic micropipette would have been more accurate. Also, the enzyme may
not have been mixed with the substrate very well. The mixing was done by inverting the test
tube before it was inserted in the spectrophotometer. This had to be done quickly because the
reaction begins immediately, but this quick mixing may not have been complete mixing. This
experiment should be repeated many times to insure accuracy of the conclusions.
LITERATURE CITED
Campbell, N.A., J.B. Reece, and L.G. Mitchell. 1999. Biology. 5th ed. Benjamin Cummings,
California.
Doordick, J.S. and J.P. McEldoon. 1996. Extraordinary Thermal Stability of Soybean
Peroxidase. Biotechnology Program 12:555-558.
Floyd, J.W. 2001. Biology 171 Laboratory Manual. Leeward Community College, Pearl City,
HI.
Ryu, K., and Y. Kim. 1997. Activation by Organic Solvents of an Alkaline Thermostable
Peroxidase / Partially Purified From Rice Hulls. Biotechnology Letters 18:1019-1022.