Emotional response to mistake leads to more improvement
COLUMBUS – Feeling the pain of failure leads to more effort to correct your mistake than simply thinking about what went wrong, according to a new study.
Researchers found that people who just thought about a failure tended to make excuses for why they were unsuccessful and didn’t try harder when faced with a similar situation. In contrast, people who focused on their emotions following a failure put forth more effort when they tried again.
“All the advice tells you not to dwell on your mistakes, to not feel bad,” said Selin Malkoc, co-author of the study and professor of marketing at The Ohio State University’s Fisher College of Business.
“But we found the opposite. When faced with a failure, it is better to focus on one’s emotions – when people concentrate on how bad they feel and how they don’t want to experience these feelings again, they are more likely to try harder the next time.”
While thinking about how to improve from past mistakes might help – this study didn’t examine that – the researchers found that people who reflect on a failure do not tend to focus on ways to avoid a similar mistake.
When asked to think about their mistakes, most people focus on protecting their ego, Malkoc said. They think about how the failure wasn’t their fault, or how it wasn’t that big of a deal, anyway.
“If your thoughts are all about how to distance yourself from the failure, you’re not going to learn from your mistakes,” she said.
Malkoc conducted the study with Noelle Nelson of the University of Kansas and Baba Shiv of Stanford University. Their results appear online in the Journal of Behavioral Decision Making.
The researchers conducted several studies. In one, 98 college students were asked to price search online for a blender with specific characteristics, and with the possibility of winning a cash prize if they found the lowest price.
Before they found out if they won, half the participants were told to focus on their emotional response to winning or losing, while the other half were instructed to focus on their thoughts about how they did. They were told they would write about their response afterward.
The price search task was rigged, though, and all participants found out that the lowest price was $3.27 less than what they found.
After writing about their failure, the students had a chance to redeem themselves.
The researchers wanted to find out if the effort put forth by participants in a new task would be related to whether they focused on their thoughts or emotions involving the previous failure. The researchers believed that a task similar to their failed job – in this case a search for the lowest price – would trigger participants into recalling their unsuccessful attempt, while an unrelated job would not.
So the participants were given another task. Half were asked to search for a gift book for a friend that was the best fit for their limited college-student budget. In other words, they were looking for the lowest price, as they were instructed in the first task.
The other half of the participants were given a non-similar task, which was to search for a book that would be the best choice as a gift for their friend.
The results showed emotional responses to failure motivated participants much more than cognitive ones when they were faced with a similar task.
Emotionally motivated participants spent nearly 25 percent more time searching for a low-priced book than did participants who had only thought about – rather than dwelled on the pain of – their earlier failure.
There was no significant difference in effort made by participants when the second task wasn’t like the first (when they were searching for the best gift, rather than the cheapest).
“When the participants focused on how bad they felt about failing the first time, they tried harder than others when they had another similar opportunity,” Malkoc said.
“But the situation has to be similar enough to trigger the pain of the initial failure.”
One reason why an emotional response to failure may be more effective than a cognitive one is the nature of people’s thoughts about their mistakes.
When the researchers analyzed what participants who thought about their failure wrote about, they found significantly more self-protective thoughts (“This wasn’t my fault,” “I could not have found it even if I tried”) than they did self-improvement thoughts (“I know how I can do better next time”).
Unfortunately, that may be the default mode for most people, at least in many everyday situations.
In another similar study, the researchers didn’t tell some participants how to respond to their failures. They found that these people tended to produce cognitive responses rather than emotional ones, and those cognitive responses were the kinds that protected themselves rather than focused on self-improvement.
Malkoc said that in most real-life situations, people probably have both cognitive and emotional responses to their failures. But the important thing to remember is not to avoid the emotional pain of failing, but to use that pain to fuel improvement.
“Emotional responses to failure can hurt. They make you feel bad. That’s why people often choose to think self-protective thoughts after they make mistakes,” she said.
“But if you focus on how bad you feel, you’re going to work harder to find a solution and make sure you don’t make the same mistake again.”
What web browsers and proteins have in common
Researchers discover molecular “add-ons” that customize protein interfaces
COLUMBUS—Researchers in the United States and Germany have just discovered a previously overlooked part of protein molecules that could be key to how proteins interact with each other inside living cells to carry out specialized functions.
The researchers discovered tiny bits of molecular material—which they named “add-ons”—on the outer edges of the protein interface that customize what a protein can do. They chose the name because the add-ons customize the interface between proteins the way software add-ons customize a web interface with a user.
While it’s long been known that proteins have an interface region where they connect with other proteins, it’s not been clear exactly how key proteins are able to find each other within a crowded cellular environment that may contain tens of thousands of other proteins.
Now, researchers at The Ohio State University and the University of Regensburg report in the Proceedings of the National Academy of Sciences that it’s the add-ons that enable proteins to connect exclusively with the right dedicated partner.
Florian Busch, a postdoctoral researcher in chemistry and biochemistry at Ohio State and co-author of the study, called the existence of protein add-ons “a previously unknown fundamental driving principle” to ensure that proteins interact in specific ways.
The researchers experimented with live bacteria, demonstrating the importance of add-ons to normal cellular functions. For example, they determined that in the organism Bacillus subtilis, in which a unique interface add-on is missing, bacteria colonies grew 80 percent less under certain conditions. The reason for this was that the missing interface add-on led to un-healthy cross-interactions of proteins in the B. subtilis cells.
It’s difficult to overstate the importance of proteins to life as we know it. Enzymes are proteins that enable chemical reactions in cells. Antibodies are proteins that bind to foreign invaders in the body. The list goes on to include thousands of critical functions. In most cases, proteins have to connect to each other and form groups called protein complexes to perform such diverse tasks.
But exactly how proteins are able to do all that they do is a mystery—one rooted in mathematics and geometry. There are 20 known amino acids which link together in long chains and then fold up to form proteins. It’s the fold that determines a protein’s generic shape, or geometry. Although there are only around 1,000 known protein geometries in nature, somehow proteins are able to form complexes that perform hundreds of thousands of very specific functions.
Maximilian Plach, lead author of the paper and biochemist at the University of Regensburg, explained how the researchers knew where to look to solve the mystery.
“Much work has been put into analyzing how proteins interact with each other and what the interfaces look like, how they are constructed, and how they evolved,” he said. “But the peripheral regions of interfaces have not received as much attention. I think the novelty in our approach was to look at regions that have been, as yet, regarded as less important.”
The Regensburg team, led by computational biologist Rainer Merkl and protein biochemist Reinhard Sterner, analyzed the protein sequences derived from more than 15,000 bacterial and archaeal genomes on a large computer cluster. They sorted proteins that shared common evolutionary ancestors into a kind of family tree, and compared individual proteins to their protein “relatives.” That’s how they spotted interface structures that were present in some proteins but missing in others—the add-ons.
Busch and Vicki Wysocki, Ohio Eminent Scholar of Macromolecular Structure and Function and director of the Campus Chemical Instrument Center at Ohio State, then used native mass spectrometry to detect how the presence and absence of add-ons influenced the ability of proteins to interact with each other.
“We’re really pleased that our native mass spectrometry technology could help identify the role of these interface ‘add-ons’—a way for a protein to find its critical partner protein even in a crowded cellular environment with similar structures present,” Wysocki said.
To Busch, one of the really exciting things about the study was the researchers’ use of “big data”—in this case, entire protein and genome databases.
“I consider our work to be one important example of how to make use of publicly available data in order to understand fundamental principles in nature, and I think that data mining will become increasingly important in the biomedical field in the future,” he said.
Co-authors on the study included Florian Semmelmann, Markus Busch and Leonhard Heizinger of the University of Regensburg. This work was sponsored by the National Institutes of Health, the Fonds der Chemischen Industrie and the Konrad-Adenauer-Stiftung.