About
Scientific research is a group activity. Independent research papers support this activity by reporting previously unobserved phenomena, new methods, or important modifications of accepted methods. As with lab reports, the goal of independent research papers is to document findings and communicate their significance. Independent research papers have an additional function, however: to develop testable hypotheses and to persuade others to accept or reject them. To do so, they present not just data, but interpretations of the data and the significance and connections found within it. Independent research papers are generally written for publication in a peer-reviewed journal, so they are tightly structured and extensively reviewed before they are released. As the author of an independent research paper, you, therefore, must be able to intellectually justify your work.
Writing Tips: Research Report
An independent research report does more than simply present data; it demonstrates your comprehension of the concepts behind the data. Merely recording expected and observed results, while critical, is not sufficient. The Discussion (or Conclusion) section is the correct place to make your research report meaningful to readers.
Make it relative.
Relate how and why differences between your hypothesis and results occurred.
Explain differences.
Give details about how any differences affected your experiment.
Demonstrate understanding.
Show your understanding of the principles the experiment was designed to examine.
Expect multiple rounds of revision.
Writing an independent research report is usually just the beginning. You can expect many rounds of review and revision, starting with your co-authors, colleagues, and other member of your organization and — with luck — continuing with the journal editor. Actively seek feedback. Do not take editorial criticism personally even though it may expose gaps in your logic or weaknesses in your design. Most reviewers simply want to help you produce a better, stronger paper and will give you good advice.
Elements of a Research Report
IMRAD is an acronym for the basic standard structure of a scientific paper: Introduction, Methods, Results, and Discussion. The simplest reports may require only these sections. Because lab reports vary tremendously in length and purpose, they may include other sections as well. It depends on your scientific field and the requirements of your class or organization. Always be sure to find out which parts your instructor or supervisor wants you to include.
Title
The Title is a label that tells potential readers what is in the report. Briefly describe exactly what you studied. Use straightforward language and keywords that researchers and Internet search engines will recognize. Most lab reports have a title.
Abstract
The Abstract helps the reader judge whether to read the whole report. Abstracts are useful when reports are long or especially complicated. Condense the entire lab report into a brief summary of no more than 200 words. Summarize each major section — Introduction, Methods, Results, and Discussion — in one or two sentences. Use those sentences to construct the Abstract, putting them into the same order in which the reader will encounter them in the final report.
Introduction
The Introduction tells the reader why your work is important. Explain why and where the study was done. What knowledge already exists about this subject? If you quote or cite previous work, number it in the text. What is the specific purpose of the study? Include this information in every report.
Materials and Methods
The Materials and Methods section helps the reader understand how you arrived at your results. Describe your study procedures. What protocol did you follow? What reagents, organisms, populations, assays, statistical conventions, and instruments were used? Why and how? For field studies, say where and when the work was done. Give readers enough detail to understand your procedure so they can repeat it. If you followed procedures from a lab book or another report exactly, just cite that work and note that details can be found there. Include this information in every report.
Results
The Results section is the core of your report, where you report your findings. Use tables (see Tables) as needed to summarize your findings. Title all tables; include a legend to explain symbols, abbreviations, or special methods. Number tables separately, if you have more than one, and refer to them in the text by their numbers. Summarize the overall findings in a sentence or two. Include this information in every report.
Discussion
The Discussion (sometimes called the Conclusion) is where you try to place your findings in a larger context and relate them to the goals stated in your Introduction.
References
The References section is the place to credit any information sources you used when writing your report. List any papers, books, websites, and other sources you cite within your report. Arrange them either alphabetically by the authors’ last names or numerically in the order in which you cited them in the text. Follow the format for citations recommended by your teacher or supervisor.
Appendices
The Appendices are where you put helpful background material that doesn’t belong in the main body of your report. Put any additional or supplementary material here. Make sure you reference material included in the Appendix where it is relevant in the body of your report.
Further Reading
The Further Reading section alerts interested readers to other related publications that they might also want to see. List these works here, alphabetized by the last names of the authors.
Note: These components vary somewhat, depending on your field and the requirements of the organization or journal. Always consult the journal publisher to find out the particular requirements for manuscripts.
See a Model: Research Report
Research Report
This article is reprinted with the permission of the corresponding author and the Society for Endocrinology.
Effect of heparin administration to sheep on the release profiles of circulating activin A and follistatin (Item 1)
Kristin L Jones, David M de Kreiser and David J Phillips
Center for Molecular Reproduction and Endocrinology, Monash Institute of Reproduction and Development, Monash University, Clayton, Victoria 3168, Australia (Requests for offprints should be addressed to D Phillips; Email: david.phillips@med.monash.edu.au) (Item 2)
Abstract
Activin A and follistatin are normally present in relatively low amounts in the circulation. Heparin administration elicits a rapid and robust release of these proteins, although this phenomenon is poorly defined (Item 3). In the present studies, the response to heparin administration was evaluated in the plasma of adult ewes in terms of whether it was dose-dependent, could be neutralized, was responsive to multiple stimulation, and the nature of the activin A and follistatin released (Item 4). Activin A and follistatin were rapidly released by heparin in a dose-dependent manner (25, 100 or 250 IU/KG), with differences in the response as judged by peak concentration, timing of the peak and area under the curve. The heparin response could be blocked by pretreatment with protamine; conversely protamine injection alone (2 mg/kg) elicited release of follistatin but not activin A. Repeat administration of heparin at three-hourly intervals resulted in activin and follistatin, but each subsequent stimulation increased and extended the responses, consistent with the saturation of the heparin clearance mechanism. Size exclusion chromatography of plasma samples confirmed that the majority of activin and follistatin released by heparin was a complex, whereas follistatin released by protamine was unbound (Item 5). These data are consistent with a large pool of activin A and follistatin resident on extracurricular matrices, with the rapid response implicating the vascular endothelium as the prime site of release following administration of these commonly used anticoagulant therapies. (Item 6)
Introduction
Activin A, a member of the transforming growth factor-β superfamily, consists of inhibin βA subunits formed into a dimer linked by disulphide bonds. Other activins are formed by dimerization of the β subunits, including activin B (βB-βB) and activin AB (βA-βB), whilst inhibin itself consists of a dimer of the inhibin β-subunit, and a β-subunit (Ling et al. 1986b). (Item 7) Activin A was first identified as an enhancer of pituitary follicle-stimulating hormone (FSH) release (Ling et al. 1986a, b, Vale et al. 1986) although subsequently, and concentrations increased immediately following the point in the surgical procedure where 5000 IU heparin were administered (Phillips et al. 2000). An analysis of the kinetics of the response in patients receiving heparin during coronary angiography procedures suggested that the majority of the activin and follistatin was released as a complex, but the disappearance curives and half-life kinetics for activin and follistatin differed (Phillips et al. 2000). The latter raised the possibility that the manner in which activin and follistatin are released, and potentially reassociate with cell surfaces, has multiple components (Item 8). The current studies were initiated to explore these responses in more detail. Specifically, the aims were to define if the release of activin and follistatin by heparin (i) was dose-dependent, (ii) could be blocked by the use of the heparin blocking agent, protamine, (iii) was altered by repeated doses of heparin, i.e. was saturable, and (iv) was largely composed of activin complexed to follistatin. (Item 9)
Materials and Methods (Item 10)
Animals and general details
All experiments were conducted in accordance with the National Health and Medical Research Council (NHRMC) Australian Code of Practice for the Care of Animals for Scientific Purposes (1997) and were approved by the Victorian Institute of Animal Sciences Animal Ethics Committee (Item 11). Adult Corriedale ewes (separate animals for each experiment) were weighed (median with 53 kg, range 44-61.5 kg), randomly allocated into groups of four animals (Item 12), and housed indoors in individual pens with access to a maintenance ration of lucerne chaff with tap water available ad libitum. The day before intensive blood sampling, indwelling catheters (Dwellcath, Tuta Laboratories, Lane Cove, Australia) were inserted into the external jugular vein under local anesthesia. A bleeding line (Manometer tubing, Tuta Laboratories) with a three-way tap was attached to allow blood sampling (Item 13). Throughout the studies, the patency of the catheters was maintained with a 0.9% saline solution containing 37 mM dipotassium ethylenediaminetetraacetic acid (EDTA, BDH Laboratory Supplies, Poole, Dorset, UK), which does not affect circulating concentrations of activin A or follistatin (Klein et al. 1996). Blood samples (5ml) were immediately spun at 250 g at 4° C in blood collection tubes containing EDTA (50 µl of 740 mM EDTA solution per tube). Plasma from each sample was stored at –20C until assayed.
Experimental Details
In a first experiment (Item 14), groups of four animals received an intravenous bolus injection of 0, 25, 100 or 250 IU/kg body weight unfractioned porcine heparin (David Bull Laboratories, Mulgrave, Victoria, Australia) in 0.9% sterile saline solution. These doses were chosen to bracket the dose of heparin (5000 IU, Williams et al. 1989) used commonly in human cardiovascular procedures (Item 15) (assuming an average ewe body.)
In a third experiment, groups of four animals received three intravenous injections of 100 IU/kg heparin or 0.9% sterile saline at 0, 3 and 6 h relative to the first injection. The treatment groups were (i) saline at 0, 3 and 6 h, (ii) heparin at 0 and saline at 3 and 6 h, (iii) heparin at 0 and 3 and saline at 6 h, and (iv) heparin at 0, 3 and 6h. Blood samples relative to each injection were collected at similar time points to that described above (Item 16). Size exclusion chromatography was performed on selected samples to provide some preliminary analysis of the composition of the activin and follistatin entities released by heparin. This method was chosen over more sophisticated methods of mode of separation because the primary question was to ascertain if activin and follistatin existed as complexes or in the unbound state (Item 17) (25 and 39-45 kDa respectively) and a complex of activin and follistatin (_100 kDa). Columns of Sephadex G-75 (Pharmacia Biotech, Uppsala, Sweden) were prepared with a bed volume of 20 ml as per the manufacturer’s instructions (Item 18). The loading and running buffer was 0.01 M phosphate-buffered saline (PBS) containing 0.2% bovine.
Assays
Activin A was measured in an enzyme-linked immunosorbent assay (ELISA) format as previously described (Knight et al. 1996). This assay measures total activin A, that is both free, and due to a dissociation step, follistatin-bound activin A. The standard was human recombinant activin A. The mean sensitivity was 0.014 ng/ml, and the mean intra- and interassay coefficients of variation were 5.1% and 5.4% respectively (Item 19). Follistatin was measured using a radioimmunoassay (RIA), as previously described.
Statistics
Statistical analyses were performed using GraphPad Prism 2.01 Software (GraphPad Software Inc., San Diego, CA USA). Activin A and follistatin concentrations were analyzed using repeated-measures ANOVA, with Dunnet’s post-hoc test where significant differences were detected. Differences in peak concentrations were analyzed by one-way ANOVA followed by the Neuman-Keuls posthoc test. Because time to peak concentration was a discrete, non-Gaussian variable, this was analyzed by the Kruskall-Wallis test, followed by the Dunnet’s post-hoc test. A significance level of P-0.05 was used in all analyses. (Item 20)
Results
Dose-response effects of heparin
Exogenous heparin over a 16-fold range elicited a rapid release of both activin A and follistatin into the circulation (Table 1). At each of the three doses, proteins were elevated within 5 min of heparin administration, consistent with a rapid release from extracellular sites (Item 21). However, the response characteristics for each heparin dose differed. (Table, not included in model)
Neutralization of heparin with protamine
To determine if the release of activin and follistatin by heparin could be blocked by administration of protamine (Item 22), the moderate heparin dose (100 IU/kg) was chosen for subsequent experiments. As shown in the first experiment, the control group injected with saline vehicle showed no significant changes in activin A or follistatin (Fig. 1a), and those animals treated with heparin showed a robust response (Fig. 1b) (Item 23). When heparin was pretreated with 2 mg/kg protamine before injection, there was no significant change in activin A and follistatin (Fig. 1c), indicating that the protamine was able to ablate the stimulatory effects of heparin. Surprisingly, however, protamine administered in the absence of heparin resulted in a significant increase in follistatin but not activin A concentrations (Fig. 1d). (Item 24) Compared with the group receiving heparin, peak.
Effect of repeated doses of heparin
To determine the response characteristics to repeated doses of heparin, animals were given either no, one, two or three injections of 100 IU/kg heparin at three-hourly intervals. (Item 25) As observed for the first experiment, a single injection of heparin elicited levels at the time of the subsequent challenge. For animals that had received three heparin challenges (Fig. 2d), activin A and follistatin concentrations 3 h after the third injection remained at peak levels. This suggested that the clearance mechanisms for heparin had become saturated. (Item 26)
Figure 2 Changes in the plasma concentrations of activin A (open circles) and follistatin (closed circles) following repeated injections of heparin or saline at 0, 180, and 360 min relative to the first injection. (a) No heparin injections, (b) heparin (100 IU/kg) at 0 min, (c) heparin at 0 and 180 min, and (d) heparin at 0, 180 and 160 min in adult Corriedale ewes. All figures and values are representative of the mean (n=4 animals)? S.E.M. (Item 27)
Composition of activin and follistatin released by heparin
Activin A present in plasma from heparin-treated ewes ran at an apparent higher molecular weight following size exclusion chromatography than human recombinant activin A (25 kDa) in PBS, suggesting it was predominantly bound to follistatin (Fig. 3a). (Item 28) When plasma was spiked with 10 ng activin A, the majority of activin.
Discussion
This study supports and extends previous findings that activin A and follistatin are released into the circulation by interactions with heparin. It has further defined the response by demonstrating a number of parameters—that it is dose-dependent and saturable; that it can be ablated by co-treatment with protamine; that, intriguingly, protamine itself can initiate release of follistatin but not activin A; that repeat responses to heparin can be achieved; and that the majority of activin A and follistatin in the circulation following heparin administration occurs as a complex. (Item 29)
Soluble heparin and its analogues can bind and displace factors such as follistatin from HSPG on cell surfaces and in the extracellular matrix. As activin A itself does not exhibit any affinity for HSPG (Yamane et al. 1998) and the release of activin A by exogenous heparin is concurrent with that of follistatin, this suggests that a significant reservoir of activin-follistatin-288 complexes exist on extracellular matrices. This is consistent with the observations that follistatin is associated with cell surfaces and that activin bound to follistatin (Item 30) accelerates the internalization and lysosomal degradation of activin-follistatin complexes (Inouye et al. 1992, Hashimoto et al. 1997). The rapidity of the release, within 5 min, would infer that it occurs from the luminal surface of the vascular endothelial cell (Hiebert & Jacques 1976, Gensini et al. 1984). It therefore seems reasonable that the rapid release of activin A and follistatin is the result of extracellular interaction of heparin with surface bound activin A and follistatin in the vascular endothelium. (Item 31) The source of this activin A and follistatin on the cell surface of vascular endothelial cells can arise from the de novo synthesis of both follistatin and activin by vascular endothelial cell sythesis and secretion (McCarthy and Bicknell 1993, Michel et al. 1996, Braumann et al. 2000). Alternatively, it could result from the `trapping’ of circulating activin-follistatin that are secreted from many cellular sources (DePaolo 1997, Welt et al. 2002). (Item 32)
Further evidence that the activin and follistatin released by heparin were bound components following heparin administration. Of interest was that there was no absolute consistency between activin A and follistatin when response parameters were examined with differing doses of heparin (Table 1). (Item 33) A possible explanation is that different populations of these proteins are released by heparin, most likely a predominant component of follistatin that is bound to activin, and a smaller proportion of ‘free’ follistatin.
The increase of follistatin and activin A following an injection of heparin could have implications for patients receiving heparin during surgery. (Item 34) Activin A and follistatin are potent multifunctional proteins in the context of cardiovascular function, with the recent finding that activin A overexpression maintains vascular smooth muscle cells in a contractile phenotype and inhibits neointimal formation (Engelse et al. 2002). A limitation with using assays that measure total activin A and follistatin for the current studies is that there is no distinction between ‘free’ and bound follistatin and activin A. Furthermore, currently an appropriate bioassay for plasma or serum activin A or follistatin does not exist. While the majority of activin A and follistatin released appeared to be complexed, as determined by chromatography, it cannot be ruled out that under some circumstances activin A and follistatin dissociate. (Item 35) The affinity of the activin-follistatin complex is very high (46.5~0.37 pM, Hashimoto et al. 2000), but previously it has been shown that following heparin administration to patients, the disappearance time for activin A is slightly faster than for follistatin (Phillips et al. 2000). Furthermore, analysis of several parameters from the dose–response studies (Table 1) showed that the upswing of activin and follistatin profiles were concordant, but the disappearance kinetics of activin and follistatin did differ slightly, suggesting that there are subtle differences in the dissociation and association processes for each protein.
The significance of our findings remains elusive and we are exploring in continuing studies whether activin A and follistatin released by heparin disappear from the circulation via multiple and possibly divergent pathways. (Item 36)
Acknowledgements
We thank Bruce Doughton, Karen Perkins, Anne O’Connor, Sue Hayward, and Lynda Foulds for excellent technical assistance. (Item 37)
Funding
This work was funded by the NHMRC of Australia (Program Grant 143786).
References (Item 38)
Bobik A & Campbell JH 1993 Vascular derived growth factors: cell biology, pathophysiology, and pharmacology. Pharmacological Reviews 45 1-42.
Boneu B, Caranobe C, Cadroy Y, Dol F, Gagaig AM, Dupuoy D & Sie. Evidence for a saturable mechanism of disappearance of standard heparin in rabbits. Thrombosis Research 46 835-844.
Boneu B, Caranobe C, Cadroy Y, Dol F, Gabaig AM, Dupuoy D & Sie P 1988 Pharmacokinetic studies of standard unfractionated heparin, and low molecule weight heparins in the rabbit. Seminars in Thrombosis and Hemostasis 14 18-27.
Brauman JN, Smith AI, Scheerlinck JP, de Kretser DM & Phillips DJ 2000 Activin A and follistatin responses to inflammatory mediators in the endothelium. Proceedings of the 11th International Congress of Endocrinology, Sydney, Australia, Abstract P512. DePaolo LV 1997 Inhibins, activins and follistatins: the saga continues. Experimental Biology and Medicine 214 328-339.
(Remaining references not included in model.)
Society for Endocrinology (2004). Reproduced by permission.
Features of a Research Report
The notes below explain more about specific components of this type of document.
Item 1. The title is descriptive, to the point, and uses keywords: the name of the drug used as independent variable (heparin), the subject (sheep), the outcome of interest (release profiles), and the names of the molecules studied as dependent variables (activin A and follistatin).
Item 2. In this case, the authors are listed alphabetically. Note that the lead author is not the contact person, and no conflicts of interest have been identified.
Abstract
Item 3. This portion of the Abstract, which identifies the background for this study, is condensed from the Introduction.
Item 4. This part of the Abstract briefly describes the Methods.
Item 5. The bulk of this Abstract summarizes the results.
Item 6. The balance of the Abstract covers the essential points in the Discussion.
Introduction
Item 7. The Introduction begins by describing the dependent variables and providing the background information that is relevant to this study. It also cites the previous work that produced this existing knowledge and credits the authors of those studies.
Item 8. Here, the authors cite the discovery that triggered their own investigation.
Item 9. The Introduction ends with the general research question, broken into four specific objectives.
Materials and Methods
Item 10. The authors cite guidelines they followed, so they don’t have to cite them in this report.
Item 11. Here, they describe their subjects and tell how they were selected and allocated to groups.
Item 12. How subjects were prepared for the intervention. The level of detail the authors provide here will enable others to duplicate their work.
Item 13. This detailed description of the equipment, the steps taken to maintain it, and the way samples were handled assures the reader that the authors designed their sampling protocol to eliminate as many potential problems as possible.
Experimental Details
Item 14. Because their experimental protocol was fairly involved, the authors have used “flags” such as “first”, “next”, and “third” to alert the reader to the different steps.
Item 15. Here, the authors describe what precisely they did in the first experiment—and why they chose the method. The other experiments are described in similar fashion.
Item 16. This section describes how the authors manipulated the independent variable. The saline is the control (placebo, or inactive treatment). Note that where they repeat a treatment they have already described, they simply refer the reader to a previous description, rather than repeating it.
Item 17. Here, the authors justify their choice of method as most likely to produce the information they seek.
Item 18. The authors don’t need to explain how they prepared the samples because the method is standard for this procedure and available from the manufacturer of the instrument.
Assays
Item 19. This section of the Methods describes the assay in detail because it is not a well-known procedure.
Statistics
Item 20. To assure that others can replicate the statistical analyses to process the data, the authors have listed the software and the standard statistical methods they used. They also tell the reader how they defined the statistical significance.
Results
Item 21. This result answers the authors primary research objective. The rest of the paragraph provides more details.
Item 22. Here, the authors remind the reader what their second objective was.
Item 23. Figures and tables are cited in the text.
Item 24. This is the answer to the second research objective. The authors also observed something they had not expected. They alert the reader to this unexpected result with the words “Surprisingly, however…”
Item 25. This sentence reminds the reader of the third research objective and the method used to achieve it.
Item 26. This is the answer to the authors third research question.
Item 27. These are notes for Figure 2. This figure eloquently illustrates the answer to the authors third research question: a quick glance shows the reader the effects of each intervention and demonstrates the differences among them. Note that every part of the figure is carefully labeled and defined, so the reader doesn’t have to guess about what the item represents. The figure legend (the text underneath the figure) provides additional information.
Item 28. This is the answer to the author’s fourth research question.
Discussion
Item 29. The Discussion begins with the answer to the primary research question and to all the research objectives. It also tells the reader how the results fit into what is already known about the subject.
Item 30. Here, the authors offer one inference that can be drawn from their work, based on what was already known. They support this possibility by citing other work that fits their logical framework.
Item 31. The authors make another inference, again supporting it with previously published work. Then, they logically connect the two inferences into a single hypothesis.
Item 32. As part of the intellectual justification for the hypothesis they have proposed, the authors suggest possible mechanisms for it.
Item 33. Here the authors alert the reader to a surprising finding and suggest propose explanations for it.
Item 34. This sentence explains the potential clinical importance of these findings.
Item 35. Here, the authors note limitations and potential weaknesses of their study. They also acknowledge that they cannot rule out certain alternative explanations.
Item 36. The Discussion end with the acknowledgment that the authors have not been able to figure out the precise clinical significance of their findings.
Acknowledgements
Item 37. If you receive substantial help from people who are not named as authors, thank them in the Acknowledgements. Disclose any funding source. (Same note for funding section)
References
Item 38. References are often—but not always—listed alphabetical order by the lead author’s name. Check with the journal and followed its preferred style. (Same for highlighted first reference.)
Revision Checklist: Research Report
Focus/Purpose
Does all of the detail and support you offer relate to your stated Research Question and Objectives?
- Check each point and detail you include against your Research Question and Objectives. Is it clear how they follow from or support your overall purpose and direction?
- Include sources that contribute to your hypothesis, or to the history of research leading up to your research. Be brief when providing sources that do not directly help the reader understand your study. Omit sources that only tangentially relate to your study. Include these in Further Reading.
- Omit arguments and details that do not directly relate to your Objectives. This does not mean that you should not include findings that are counter to your hypothesis — determine the difference between relevant counter-evidence and irrelevant detail.
Development/Elaboration
Have you named all the Authors of your paper and provided pertinent information about them?
- List everyone responsible for the intellectual content of the paper.
- Give the first name, middle initial, and last name of each, with their academic degree.
- List author affiliations and disclose any conflicts of interest.
- Provide contact information.
- Identify your funding sources and other providers of material help.
Does your Abstract emphasize a summary of the Results and Discussion?
- Make sure your work is described clearly, comprehensively, and accurately.
- For biomedical papers, provide key terms drawn from the Medical Subject Headings (MeSH) list of Index Medicus.
Does your Introduction set up the background and rationale for your study?
- Start with your problem statement.
- Explain what prompted your study.
- Provide non-specialists enough information to understand the problem.
- Summarize credible published studies about your topic.
- Explain why previous studies have not answered your research question.
- Explain how your study design may produce more useful results.
- Provide background that supports the rationale for your methods.
- End with your research question, both your main objective and secondary ones.
Have you fully explained your Materials and Methods?
- Describe your study design and protocol.
- Provide the general theory of the analyses or assays you used.
- Detail how you selected the phenomena, organisms, or populations you studied. Describe interventions or treatments in detail.
- Say what you measured, and how.
- Specify the statistical methods you used.
- Define your cutoff for statistical significance.
Do your Results answer the research question clearly?
- Give as clear an answer as your data will permit.
- Account for all subjects you enrolled.
- Report any surprising findings.
- Show how previous reports corroborate your data.
- Cite all your sources.
- Include tables, graphs, and figures.
- Provide subheads as needed to organize your content.
Does your Discussion examine your Results carefully enough?
- Open with the answer to your research question.
- State whether or not the overall results support your hypothesis.
- Give the central conclusion that can be drawn from your data.
- Cite work by others to support your conclusions.
- Present and assess counter-evidence.
- Note any possible reasons for unexpected results.
- Suggest new avenues for research on your topic, based on your results.
- Suggest ways that your techniques or experimental design could be improved. Close by restating the answer to your research question.
Are your References complete, and correct?
- Follow the recommended format for the journal.
- Avoid using and citing unpublished observations and personal correspondence.
- Ensure that all studies are cited correctly.
Organization
Do you arrange your paper to introduce the points you make then provide detail and support? Is the purpose and topic of each paragraph clear and well-supported?
- State your Research Question or Hypothesis and primary objectives early in your paper.
- Start each paragraph with a topic sentence that tells the reader what you are going to address.
- Logically arrange support within each paragraph.
- Use transitions to make connections between sentences and paragraphs.
Style
Do you use terminology and styles that are appropriate to your field?
- Follow the writing style of other works in your field. Read other articles to get a feel for how they express ideas.
- Avoid contractions (didn’t, it’s), abbreviations, and slang.
- Use technical terms from your field. Define terms that may not be commonly understood by your audience.
How to write for your audience - Follow the required style of your class or journal.