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[su_heading size="15" margin="0"]The BioInnovation Group is an undergraduate-run research organization aimed at increasing undergraduate access to research opportunities. We have many programs ranging from research project teams to skills training (BIG-RT) and Journal Club.

If you are an undergraduate interested in gaining research experience and skills training, check out our website (https://bigucd.com/) to see what programs and opportunities we have to offer. In order to stay up to date on our events and offerings, you can sign up for our newsletter. We look forward to having you join us![/su_heading]

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Through War and Peace, These Doves Rock

By Daniel Erenstein, Neurobiology, Physiology & Behavior ‘21

 

“The diversity of the breeds is something astonishing,” Charles Darwin wrote in “On the Origin of Species.” He was not referring to his famous Galápagos finches. Instead, Darwin opened his foundational work by commenting on various breeds of the domestic pigeon, all descended from a common ancestor: Columba livia. Widely known as the rock dove, this species has adapted to urban environments throughout human history. Over time, we have kept pigeons for fairs, racing, message carrying in wartime, and even scientific research.

Since joining the B3 Lab at UC Davis in 2020, I have contributed to research on this model organism. The B3 name, short for Birds, Brains, and Banter, represents the lab’s main goals: to study rock doves and how stress affects their reproductive behaviors, and to advance culturally relevant science communication research and training. In April, I presented a project on how single parenting affects the amygdala, often considered the brain’s “emotional center,” at the UC Davis Undergraduate Research, Scholarship, and Creative Activities Conference. This research helps us to understand the impacts of single parenting in humans, and it could lead to insights that mitigate stresses felt by single parents and their children.

These photographs were captured in the B3 aviary via iPhone 7 camera during 2020 and 2021.

 

Environmental Effects of Habitable Worlds on Protein Stability

By Ana Menchaca, Biochemistry and Molecular Biology ‘20

Author’s Note: As a biochemistry major hoping to further pursue an academic career in astrobiological research, this paper jumped out at me when finding a topic for a class assignment. It goes to show just how many paths there are to take in investigating life elsewhere in the universe and how much we still have yet to discover and understand. 

 

The search for life elsewhere is a vast, challenging undertaking, and investigation of conditions on so deemed habitable worlds provides insight into our current understanding of the existence of life. The conditions for a world to be considered potentially habitable are similar to those of life on Earth. These conditions include a source of energy, common essential elements that make up life (carbon, hydrogen, nitrogen, oxygen, phosphorus, and sulfur), and a solvent for chemical interactions (e.g. H2O). Understanding how chemicals and molecular components might interact with these environments can provide us with a better understanding of what could actually hold the potential for life as we currently know it. One of these important molecular components is proteins. 

Research exploring protein stability on Saturn’s largest moon, Titan, published in November 2019, presents an early foray into these considerations. This research studies the implications of variable environmental conditions on protein interactions and how this could detect potentially habitable worlds, similar to Earth. The study makes a foray into studying whether the conditions deemed necessary on Earth are really necessary for the survival of proteins. Molecular dynamics simulations explored structural interactions based on our current knowledge of protein interactions, using the software package GROMACS [1]. 

Titan is one of these potentially habitable candidates in our solar system, a category that also includes several other moons: Europa, Enceladus, Ganymede, and Callisto. All of these moons are considered to have subsurface oceans present, conditions that have the potential for the presence of chemical building blocks, liquid H2O, and sources of energy. Models show that Titan’s subsurface oceans may contain hydrogen, carbon, nitrogen, and ammonia (ensuring that the oceans remain liquid), thus indicating the potential for Earth-like biochemistry [1]. 

Martin et al. explored the potential effects of Titan’s hypothesized environment on the integrity of biologically relevant molecules. Protein compactness, flexibility, and backbone dihedral angle distributions were measured. Because protein folding is affected by affinity and electrical interactions with the environment that they’re in, the difference in the conditions of Titan’s high-pressure subsurface oceans to those on Earth has the potential to affect the folding and behavior of relevant proteins [1]. Even on Earth, extremophiles in hydrothermal vents have varying versions of common proteins, something that could indicate the potential for novel protein conformations that perform similar functions in unique, more extreme conditions than those on Earth. The potential existence of these conformers, which still act and provide the same structures and functions of Earth proteins, broadens and changes our scope of what’s necessary and indicative of life. 

In comparing Titan-like conditions to Earth, Martin et al. observed variations in the behavior of selected proteins (which were selected to highlight common folding of alpha helices and beta sheets). Proteins are formed at various levels of structure: primary, secondary and tertiary. The primary structure is the amino acid sequence, secondary structure is created by interactions of the polypeptide with itself, and tertiary structure is the proteins three dimensional, overall folding. Alpha helices and beta sheets are the most prevalent secondary structures for proteins on Earth, and the complex interactions and stability of these structures drives many biochemical interactions. 

The Root-mean-square fluctuation, or how much the atoms fluctuated about their average position, of the proteins in Titan-like conditions was lower on average than that of the proteins on Earth, indicating less variability in structure in these conditions. Additionally, for one of the proteins, rather than not stabilizing into a specific secondary structure like on Earth, it instead settled into a pi helix conformation, a secondary structure that’s uncommon on Earth, as it is less stable [1]. Due to this lack of stability compared to alpha helices, they are typically found near functional sites.These varying secondary structures of proteins affect their ability to interact with other molecules and enzymes in complex ways, something that in the case of pi helices is less explored given their relative rarity on Earth. 

These results show that while beta-sheets show similar behavior and presence in Titan-like conditions as they do on Earth, there’s also a tendency towards less common conformations (pi helices). These results expose both this variation of protein conformation and shape in differing conditions, and the survivability of proteins in non-Earth environments. This shows the possibility of discovering life in forms we are unfamiliar with, while also proving proteins, a vital component of life, are capable of existing in extraterrestrial environments. This research helps prove that those planets deemed habitable really are such, and the further study of the specific conformations and interactions of these proteins could provide us with more specific knowledge of what we might identify elsewhere. While this research is an early exploration of potential conditions on Titan and potentially other bodies with subsurface oceans, it still opens the door for further studies of environmental effects on known life, thus expanding our understanding of the potential for life to exist elsewhere.

 

Sources

  1. Martin, Kyle P., Shannon M. Mackenzie, Jason W. Barnes, and F. Marty Ytreberg. “Protein Stability in Titans Subsurface Water Ocean.” Astrobiology 20, no. 2 (January 2020): 190–98. https://doi.org/10.1089/ast.2018.1972.
  2. Abrevaya, Ximena C., Rika Anderson, Giada Arney, Dimitra Atri, Armando Azúa-Bustos, Jeff S. Bowman, William J. Brazelton, et al. “The Astrobiology Primer v2.0.” Astrobiology 16, no. 8 (January 2016): 561–653. https://doi.org/10.1089/ast.2015.1460.

Aggie Transcript Interview—Dr. Walter Leal

By Bukre Coskun, Cell Biology, ‘18

Author’s Note:

“As a student in Professor Walter Leal’s biochemistry class, I was inspired by his dedication to motivating students and obvious enthusiasm for his field of research. Professor Walter Leal has achieved international recognition for his research on the molecular basis of insect communication and insect olfaction. Leal, a professor in the UC Davis Department of Molecular and Cellular Biology and former chair of the UC Davis Department of Entomology, has made significant strides towards understanding how chemicals deter mosquitos. He has identified key mosquito receptors that can guide the development of better mosquito repellents to prevent the spread of deadly diseases. He is a past president of the International Society of Chemical Ecology, an elected fellow of the American Association for the Advancement of Science (AAAS), and the first non-Japanese scientist to earn tenure in the Japan Ministry of Agriculture. I had a conversation with Professor Leal about his path to research, his philosophy on teaching, and the significance of his work with insects.”

(more…)

Winter Seminar 2016: “Science Journalism and Editing: The Aggie Transcript”

The Aggie Transcript is offering its first-ever seminar on science journalism and editing in Winter Quarter 2016! Please see the flyer below for more information.

To read more about the course description, the goals of the seminar, course assignments and grading criteria, please visit the link and click “Seminar Schedule: Winter 2016”

Link: http://fys.ucdavis.edu/student/#frs-schedule

Winter Seminar 2016 Flyer-page-001(1)