Visit with the Senior Research Editor

Author:  Alexander Patananan
Institution:  UCLA

A well organized abstract packs a powerful punch.

I don't know about you, but I frequently find myself reading or watching the cartoon called "Peanuts" by Charles Schultz whenever I have free time. In several of these cartoons, one of the main characters, named Lucy, demands that Linus change the television channel and threatens him with her fist if he does not do as she says.

"What makes you think you can walk right in here and take over?" Linus frequently responds.

"These five fingers," states Lucy. "Individually they're nothing, but when I curl them together like this into a single unit, they form a weapon that is terrible to behold."

"Which channel do you want?" asks Linus quickly. Turning away, he looks at his own fingers and says, "Why can't you guys get organized like that?"

Although seemingly comical at the outset and unimportant, what Lucy says in this scene of the cartoon is what we should all be doing when we write an abstract to a scientific research or review manuscript. The abstract of a paper is the first portion of your presentation that a reviewer or reader sees. It is the make or break point. If you fail to grab the reader's attention with the abstract, chances are the reader will not bother to continue through the rest of your paper. This sounds rather harsh as many people frequently spend months, if not years, conducting experiments to put into manuscripts. But, in today's fast paced society with everyone having a very constrained time schedule, it is rather absurd to think that someone will just read your research no matter how it is written or presented. Speaking on behalf of editors, not only for JYI but also other journals, if you fail to present a good abstract it is highly probable that your paper will be rejected since it does not engage or provide information in a compact and efficient manner. Therefore, let spend a few moments to show step-by-step what makes up a good abstract that will be highly publishable. Let us take a look at the following abstract.

The adsorption and unfolding pathways of proteins on rigid surfaces are essential in numerous complex processes associated with biomedical engineering, nanotechnology, and chromatography. It is now well accepted that the kinetics of unfolding are characterized by chemical and physical interactions dependent on protein deformability and structure, as well as environmental pH, temperature, and surface chemistry. Although this fundamental process has broad implications in medicine and industry, little is known about the mechanism because of the atomic lengths and rapid time scales involved. Therefore, the unfolding kinetics of myoglobin, β-glucosidase, and ovalbumin were investigated by adsorbing the globular proteins to non-porous cationic polymer beads. The protein fractions were adsorbed at different residence times (0, 9, 10, 20, and 30 min) at near-physiological conditions using a gradient elution system similar to that in high-performance liquid chromatography. The elution profiles and retention times were obtained by ultraviolet/visible spectrophotometry. A decrease in recovery was observed with time for almost all proteins and was attributed to irreversible protein unfolding on the non-porous surfaces. These data, and those of previous studies, fit a positively increasing linear trend between percent unfolding after a fixed (9 min) residence time (71.8%, 31.1%, and 32.1% of myoglobin, β-glucosidase, and ovalbumin, respectively) and molecular weight. Of all the proteins examined so far, only myoglobin deviated from this trend with higher than predicted unfolding rates. Myoglobin also exhibited an increase in retention time over a wide temperature range (0oC and 55oC, 4.39 min and 5.74 min, respectively) whereas ovalbumin and β-glucosidase did not. Further studies using a larger set of proteins are required to better understand the physiological and physiochemical implications of protein unfolding kinetics. This study confirms that surface-mediated unfolding can be described by experimental techniques, thereby allowing for the better elucidation of the relationships between the structure and function of soluble proteins as well as other macromolecules.

In a nutshell, an abstract should explain the following points. First, always provide a little background on your research. This can usually be done in one or two sentences (in this case two sentences are used) to illustrate the fundamental aspects of your research. Second, take one sentence to explain a gap in knowledge that your paper addresses. In our example here, little is known about protein unfolding because of the associated atomic lengths and rapid time scales involved. Third, follow up this sentence with a statement concerning what you are exactly doing to fill in this gap. A good transition statement is typically "Therefore, X and Y were done in order to..." Forth, give an extremely brief overview of your materials and methods. This is typically one or two sentences that explain only the very important aspects of your experimental procedures. Fifth, state one or two sentences concerning only the most important of your results. Do not list an endless amount of data as this simply bores your reader. Also, the abstract is simply a taste of what is still to come in the rest of your paper! Sixth, state the conclusion of your paper in one sentence and follow it up with one final sentence on the future directions of your studies. If you follow these procedures when you prepare your abstract, I guarantee that your paper will have a greater chance of getting published.

If you have any questions on how to write better, feel free to contact me at Also, stay tune to next month's Visit with the SRE editorial and learn how to write that perfect introduction! Also, on behalf of the JYI team, happy holidays and have a happy New Year!