Everything You Need to Know about BPS Travel Awards

A month and a half remains before the abstract submission and travel award application deadlines for the Biophysical Society’s 62nd Annual Meeting, being held in San Francisco, California, February 17-21, 2018. If you are a student, postdoc, early or mid-career scientist looking for a little extra funding to attend the Annual Meeting, be sure to apply for a BPS Travel Award. Check out the FAQ below to learn more about the application process.

Q: What is the Travel Award application deadline?
A: The application deadline is October 4, 2017. Remember: You MUST submit an abstract by October 2 in order to be eligible for a Travel Award.

Q: Do I need to register for the meeting and submit my abstract prior to submitting the travel award application?
A: If you are applying for a travel award, you must be the presenting author on an abstract submitted by the October 2 abstract deadline (if applying for a mid-career CPOW or Bridging award, you may be presenting or senior author). You do not need to register prior to submitting a travel award application. However, you will need to register for the meeting in order to attend.

Q: Can I submit any part of my application late?
A: No. ALL parts of your application are due by the October 4 deadline – including your letters of recommendation! Start asking your advisers for references now, and be sure to read each award’s description so you know exactly what is required.

Q: I think I’m qualified for multiple Travel Awards. Can I apply for more than one?
A: Yes, you can apply for multiple travel awards, as many as you are eligible for. However, you can only be selected to WIN one award.

Q: I am a co-author on an abstract, but not a presenting author. Can I apply for a Travel Award?
A: For all Education, CID, and International awards, you MUST be a presenting author on the abstract. If you are not a presenting author, your abstract will be marked as ineligible. This also applies to CPOW awards for postdocs. For mid-career CPOW awards and Bridging funds, you must be either presenting or senior author on a submitted abstract.

Q: My adviser would rather send the letter of recommendation directly to you. Where exactly should he/she send it?
A: Letters of recommendation can be emailed to travelawards@biophysics.org.

Q: I am not a US citizen or permanent resident, but I am still a scientist from a group underrepresented in biophysics researching in the US. Why can’t I apply for the CID Travel Award?
A: Because the CID Travel Awards are funded by an NIH grant, only US citizens or permanent US residents are eligible. Please be sure to check out the Education and CPOW awards and Bridging Funds requirements to see if you qualify.

Q: I’m originally from outside the US, but I now live/research/study in the US. Am I eligible for an International Travel Award?
A: No, you are not eligible. You must be living and conducting research OUTSIDE of the US in order to qualify for an International Travel Award. If you live/work/study in the US, no matter your origins, you are not eligible for this award.

Q: I am currently a graduate student. However, by the time of the Annual Meeting I will be a postdoc. What award should I apply for?
A: You should apply for the awards that fit your career level as of October 4, 2017. In your case, you must apply as a graduate student.

Q: I am no longer a student or a postdoc. Am I eligible for a Travel Award?
A: CID, CPOW, and the International Relations Committee all offer travel awards for junior, senior, and/or mid-career scientists. Please check eligibility requirements online to see if you qualify for any of these awards. Additionally, Bridging Funds are available for independent or principal investigators who would normally attend the meeting but cannot due to lack of funding.

Q: If I do not receive a travel award to the Annual Meeting, may I receive a refund for my abstract submission and registration?
A: No, abstract submission fees are non-refundable. If you wish to retract your registration, you will be refunded the registration fee, less the $50 cancellation fee, if your request has been received by the January 15 deadline and you did not pay the combo fee.

 

Trailblazing Cells are Moving On

BPJ_113_3.c1.inddThe extracellular matrix (ECM) provides important structural support for cells in multicellular tissues and it also plays a role in guiding migration. For example, aligned matrix fibers can provide routes for directed movement. Cells can interact with their surrounding ECM biochemically as well as physically, but can cells steer the direction of these fiber tracks and how does this happen in real time? We studied the dynamics and mechanisms of matrix alignment around engineered three-dimensional (3D) multicellular tissues prior to migration and found that tissue-derived forces in the form of cytoskeletal tension are primarily responsible for rapidly aligning matrix fibers by applying strain to the ECM in a matter of hours. This process results a pattern of fibers oriented perpendicular to the tissue surface, which can then serve as directed paths for subsequent cell migration outwards from the original tissue geometry. Cells can indeed form tracks in a specific direction prior to migrating!

The cover for the August 8, 2017 issue of Biophysical Journal is an image of a 3D multicellular fibroblast tissue undergoing collective migration captured by Alexandra Piotrowski-Daspit; it was taken while she was a graduate student at Princeton University. The fibroblasts are seen migrating along collagen fibers that were initially aligned radially around the tissue surface via tissue-induced strain. Strikingly, the migration pattern is also radially outwards from the tissue that was originally circular in geometry (~100 mm in diameter). The tissue was imaged at focal planes spanning its entire depth (~50 mm) using confocal fluorescence microscopy with a 40×oil-immersion objective. The actin fibers in the fibroblasts are represented in pink. Collagen fibers in the ECM are shown in green and were visualized using confocal reflectance microscopy. The two channels were merged and the confocal stack was projected onto one two-dimensional (2D) image.

Our study revealed that coordinated cytoskeletal contractility within multicellular tissues drives ECM alignment regardless of cell type, as we noted the same behavior in normal epithelial, breast cancer, and fibroblast cells. Moreover, tissue-induced fiber alignment always precedes migration. The ability of cells to rapidly align their matrix prior to migration is likely to aid in quick reactions to changing microenvironmental cues. Further, we confirm the importance of biomechanics in the physical interplay between cells and their surrounding matrix. Our results have wide-ranging implications, as cell migration is a key biological process used during normal tissue development, wound healing, and cancer invasion.

—Alexandra Piotrowski-Daspit, Bryan Nerger, Avi Wolf, Sankaran Sundaresan and Celeste Nelson

Reasons You Should Meet with Your Congressional Representatives this August

congressional district mapAccording to a Pew Research Center Poll, 76% percent of Americans think that scientists act in the best interest of the public, and 67% think science has had a mostly positive effect on society.  In addition, despite recent headlines, the study shows that confidence in the scientific community has remained steady for the past 40 years.

At the same time, 70% of Americans can’t name a living scientist based on a 2013 poll conducted by Research!America.

In Congress, there is currently only one PhD level scientist, Bill Foster, a physicist representing Illinois i the House. There is one mathematician, Jerry McNerney from California, a handful of medical doctors, and a few political scientists.

Congress has several science-related policy issues on its plate including funding for science agencies, regulations and policies related to climate change, and support for renewable energy programs to name a few.

So what does this mean for you,, a practicing scientist?  It means that Congress needs to hear from you!

In particular, the Senators from your state and the Representative from your district need to hear from you. They need to know that you, a constituent, cares about these issues, that you,  your students, and your colleagues are affected by the policy choices they make in Washington, and that these choices can also affect the local economy.

They need to know that someone is watching and that someone cares.

The Biophysical Society wants to make it easy for you to connect with your elected officials.  This August, society staff will walk you through the process of setting up a meeting and preparing for that meeting.

All you have to do is sign up for the BPS Congressional District Visits program by July 26 and a BPS staff member will be in touch. You won’t have to travel far, and you can make a big difference.

Get out of the lab and be an advocate for biophysics!

 

 

 

 

Mesoscopic Adaptive Resolution Scheme toward understanding of interactions between sickle cell fibers

BPJ_113_1.c1.inddSickle cell disease (SCD) is a molecular disease that affects hemoglobin. To understand the altered morphologies and mechanical properties of sickle red blood cells in SCD, it is important to investigate polymerization of the mutated form of hemoglobin (HbS) and subsequent interaction with the red blood cell (RBC) membrane.

The cover image for the July 11 issue of the Biophysical Journal is an artistic rendering of several RBCs and a white blood cell in the blood flow. Some RBCs are sickle-like shape. The largest RBC in the bottom left corner is shown in the protein level. The red, blue, and green particles represent the lipid particles, spectrin proteins, and actin junctions in the RBC membrane, respectively. Inside the RBC,  a single HbS fiber consists of 14 chains of HbS tetramers arranged in a 7 double-stranded configuration. The 14 chains of HbS tetramers are twisted about a common axis in a rope-like fashion. In the image, one small yellow particle is one HbS molecule, and  56 small particles are coarse-grained as one large yellow particle.

As shown in the image, the proposed hybrid HbS fiber model seamlessly couples these two HbS fiber models at different length scales by applying a mesoscopic adaptive resolution scheme (MARS). The stiff HbS fibers interact with the RBC membrane and distort the RBC to the sickle shape. Sickle RBC morphologies are determined by the number of HbS fiber domains and the structure of each domain inside the cells. In return, the RBC membrane also suppresses the growth of the HbS fiber. In addition to irregular shapes, sickle RBCs are characterized by increased cell rigidity due to intracellular fiber structures, resulting in blood flow impairment and vaso-occlusive crises in the microcirculation.

This cover was inspired by the pressing need to understand the integrated process of HbS nucleation and polymerization, and subsequent alterations of cell morphology, which is a multi-scale process ranging from nanometers to micrometers. In order to accurately describe this process, the hybrid HbS fiber model is employed to capture the dynamic process of polymerization of HbS fibers, while maintaining the mechanical properties of polymerized HbS fibers, thus providing a means of bridging the subcellular and cellular phenomena in sickle cell disease.

—- Lu Lu, He Li, Xin Bian, Xuejin Li, and George Em Karniadakis

Alumni Spotlight -Jun Seok Lee


IMG_7233Tell us about where you are now in your academic career.

I recently graduated from Rutgers University with a double major in theoretical physics and mathematics. Come September, I will be starting a masters program in biophysics at the Université Pierre et Marie Curie (Paris VI) in France. I plan to continue towards a PhD at the end of my masters, either staying in Europe or maybe somewhere stateside where it’s always warm, like California.

What is your research focus?

I’ve spent most of my time as an undergrad exploring research options more than focusing on any specific thing. I’ve done research in high-energy experimental particle physics, in neurobiology, in genomics, and extremely briefly in optics. At the moment, I am not obligated to any specific field of research, but I am being drawn more and more towards neurophysics in regards to understanding and treating neurodegenerative diseases, as well as aspects of membrane biophysics.

When and how did you first become interested in this type of research?

I had some health issues regarding my nervous system a few years back and was really frustrated at the lack of answers and solid methodologies in diagnosis. While that frustration was more owed to my lack of patience, it did spark my curiosity in reading up on biophysics and neurophysics in general and prompted my desire to return to school to pursue my degree.

What was the most important thing you learned or took away from the summer program that helped you get where you are at now?

The summer program taught me that a PhD program is not some cutthroat outdo-your-peers competition, but rather it is a support group that is trying to help its members succeed academically, socially, and mentally. It showed me that people ranging from administrators, mentors, peers, and even unaffiliated people like professors from different departments are all willing to offer their time and support even if you don’t do anything related to what they are doing.

The program also exposed me to various types of work being done in biophysics. I had a better understanding of what work was being done in the field, and helped me both broaden and narrow my vision in the type of work I hope to pursue in my career in biophysics. The guest lecturers, the alumni, and the one-on-one counseling I received from various people both related directly and indirectly, was formative in creating the idea of what I believe is my future career goals.

What was your favorite thing about the summer program?

If not all the wonderful food (I’m not even joking here), it has to be all the people I met. My fellow students, the TAs, Mike, Barry, Lisa; everyone had a part in creating the awesome time I had during the program. I was exposed to so many types of personalities and lives a scientist could live, and I received so much good advice that has helped me get to where I am now and will probably continue to advance my growth as a scientist. I believe that during that short span of time, I was able to make connections, find new friends and mentors who I could depend on for support throughout my academic and professional career, and well into the rest of my life. Biophysics is such a broad field, and it requires a vast pool of knowledge to answer the questions posed in it. The program made it such that we all came from widely differing academic fields so that we could work together during our time in the program as well as call on each other for support for our individual work.

However, let me repeat once again, the food was great. I have cravings for that vinegar-based North Carolina barbecue sometimes.

What advice would you give for current undergraduates interested in pursuing a higher degree?

It’s not about how intelligent you are or how easily you can grasp the topic, but about persistence and consistency. Many people fall into this trap where they think just because they’re not the smartest or the fastest among their cohort, that they aren’t good enough for graduate school or beyond. Absolutely not true. You might have to put in some extra hours with the book or at the lab, but if you can hunker down and get working, consistently and diligently, you most definitely can reach that higher degree.

Have mentors played a role in your success? If so, how?

Absolutely, yes. I had multiple mentors during the program. Some were obvious mentors, and some not so much. I think you have to really take advantage of everything the program offers, whether that’s advice from your post-doc lab mentor about the research, or from a TA who was just recently in your shoes, or from a professor you sit down for conversation over lunch who tells you about how he got to where he is today, or even just passing by an office of one of the administrators and having a small chat that leads into something deeper. In whatever situation, summer program or not, there will be people out there who can help you figure out how to orient your compass.

What have been some of your toughest challenges so far in advancing your career?

Trying to figure out where my true passions lied in regards to the field I wanted to pursue. Luckily, the professors and programs I’ve applied to and been a part of have been more than helpful in guiding me towards my goal rather than trying to make me settle for any one specific thing.

Another tough thing is trying to get over what is commonly known as “imposter syndrome.” You study, you do your problem sets, you do research, but that fear of not being good enough makes you feel like you’re a fraud. That’s another thing the program helped with, is that I got to meet people along the various stages of a career path, whether in academia or industry, and it showed me that this is what everyone goes through, and as I said before, persistence and consistency are the keys to success.

BPS Summer Program Alumni spotlight


20170617_191504Hi, my name is Lonzie Hedgepeth. I am from Rocky Mount, North Carolina. I recently graduated with a Bachelor of Science in Chemistry from the University of North Carolina at Pembroke. Last year, summer of 2016, I attended the Biophysical Society Summer Research Program in Biophysics. I learned about the Biophysics Program through the help of a guest speaker in my genetics class.

My professor, Dr. Conner Sandefur, invited Patrick McCarter to talk about the biophysical properties of DNA, and how mutations in DNA can lead to diseases such as Cystic Fibrosis. Patrick’s lecture, which not only deepened my insight into the fields of biophysics and genetics, exuded vigor and confidence. After the talk, I approached Patrick. We talked about possible summer research opportunities that are available at University of North Carolina-Chapel Hill and then exchanged contact information. Later that day, I sent him an email, thanking him for a wonderful and informative seminar.

Soon after, Patrick contacted Dr. Sandefur, informing him about the Summer Research Program in Biophysics at the University of North Carolina at Chapel Hill. Dr. Sandefur and Patrick, who had attended the program himself, thought that this program would be an ideal program for a budding research scientist, such as myself, to gain extensive research experience in an environment that would mirror that of Biochemistry and Biophysics Ph.D. programs. Fortunately, I got accepted! After meeting with my cohort, I realized that we were a very diverse group, coming from different backgrounds. At first I was a little nervous, but over time the cohort and I became very close and connected like a family.

During the summer course, I was able to conduct graduate level research, attend lectures and seminars hosted by UNC-Chapel Hill faculty, participate in several professional developments activities, and also socialize with people at similar stages of their academic careers. I conducted my research in the lab of Dr. Timothy Elston, a professor in the department of Pharmacology. My direct research mentor was Patrick McCarter, who at the time was a graduate student in the Elston lab. I never expected to be working alongside Patrick, someone who I greatly admired. We worked on investigating Mitogen-Activated Protein Kinases (MAPKs) in budding yeast. We wanted to define time-dependent interactions between the Sln1 and Sho1 branches of the yeast (S. cerevisiae) High-Osmolar Glycerol (HOG) pathway. Each branch transmits hyper-osmotic stress through a MAPK cascade to Hog1 the terminal Mitogen-Activated Protein Kinase of the HOG pathway. My role in this project was to use mathematical models to investigate the time-dependent contribution of each branch to Hog1 phosphorylation (MAPK are typically active when phosphorylated). I defined a set of 24 mathematical models that each tested a different hypothesis about the time-dependent contributions to Hog1 activity. Mathematical models provide us with a way to investigate aspects of the biology that are currently not feasible with experiments alone. I then used UNC-Chapel Hill’s Killdevil High-Performance Research Cluster to ‘fit’ each model to an experimental Hog1 phosphorylation training data set. The best ‘fitting’ models were then used to predict how Hog1 phosphorylation would change under different experimental conditions including dynamic hyper-osmotic stress and/or with various genetic perturbations in key HOG pathway signaling proteins.

With the help of Dr. Elston, Patrick, and my colleagues, I was able to present my findings at Annual Biomedical Research Conference for Minority Students (ABRCMS). In addition to presenting my project, during ABRCMS I was also able to attend seminars, participate in networking, and learn about a variety of potential PhD programs.

While I mainly focused on computational science in the Elston lab, the interdisciplinary nature of the project and the collaborative research environment also allowed me to directly communicate with the experimental biologists who were gathering data needed to build the models. Thus, I learned a great deal about cellular and molecular biology, live-cell microscopy, and genetics.

Working in the lab allowed me to see how graduate students, post-docs, and senior professors manage their time, maintain organized lab spaces, and communicate their unique perspectives in an interdisciplinary research group. I was able to witness how modern scientists work together to solve some of the most interesting questions in the world. I am now using these experiences, along with the skills I accumulated from the Biophysics program, to further prepare myself to apply for Ph.D. programs in the fields of Pharmacology, Biophysics, and/or Systems Biology.

I am currently in a Post Baccalaureate Research Education Program (PREP) at Medical University of South Carolina (MUSC). I have kept in touch with Dr. Elston, Patrick, and also Dr. Sandefur! I have developed an invaluable relationship with them. They have become more than just mentors to me. I hope to emulate their perseverance and dedication to help others. They have inspired me to reach out and share my experiences to other young scientists, and to encourage them to pursue their dreams to conduct high-quality biomedical research. I am also extremely grateful to have attended the Summer Research Program in Biophysics. Through this experience, my aspirations of conducting high-quality research are immensely strengthened, and my relationships with scientists developed and flourished. I look forward to the day when I am able to help a young and budding scientist get started on their own journey in science!

New probes, singularities, and a reason for RNAi mismatches in vivo (Part 2)

Me in the rain.jpg

Me, Michael Shannon, in rainy Taipei

Takeharu Nagai (part 2/2): Singularities in cells: leaders, followers and citizens

Takeharu describes a familiar situation. Our results, whether its molecular behaviour or cellular behaviour are generally an averaged description of phenomena. We get an idea of what’s going on, but ignore the minority phenomena: the singularities that lead to group behaviours.

After a brief rundown of things he considers singularities: the big bang, the benign to malignant switch, formation of iPS stem cells with only 4 genes altered, populist fascism under Trump etc, he sets out to investigate this idea armed with a plethora of new fluorescent probes, and some cool model systems.

Here, he focuses on cAMP signalling in social amoeba, which transition from single celled entities to an intercommunicating mass, a multicellular being. To initiate this switch, all you have to do is starve them of nutrients.

By using two markers, Flamindo2 (Odaka) and R-FlincA (Horikawa, in press) he derives a ratiometric measurement for cAMP activity, known to be associated with this switch in amoeba behaviour. Combining this with a high speed microscope tiling technique, he is able to look at the behaviour of both single cells and the whole population of cells.

What he finds is amazing – single amoeba cells become leaders, displaying a burst of cAMP, before setting off their neighbours. “Early followers” then signal to “late followers”, and within a matter of hours, to “citizens”, setting off a continuous spiral of cAMP signalling which causes the amoeba to group together and become multicellular. The fluorescence videos of this are quite amazing – and while the paper isn’t out yet, you can view some similar behaviours online at Take’s website.

Interestingly, several leaders seem to be selected, but only one gains ultimate dominance as the seed of the spiral of signalling. One of the goals of the Nagai lab now is to find out how this leader is selected.

Okay, next up, Sua Myong

Sua Myong – How does RNAi actually work?

Sua employs FISH, a super resolution technique, to view RNA interference in single cells. What she finds is the first insight into the function of RNAi with reference to biologically relevant miRNAs since Fire and Mello won the nobel prize for the work and revolutionised the field.

The investigative technique works by targeting particular mRNAs with search RNAi strands loaded with 30 to 40 fluorophores each. By watching the transient binding of these RNAs in TIRF, the PSFs can be localised and the relative number of RNAs between conditions can be quantified.

The group tried to figure out which parts of shRNA were important in terms of its structure and its interactions with DICER and RISC, the proteins that bind it to genes of interest and cut the genes, respectively. To do this they altered the shRNA supplied to the cell by first changing the size of the hairpin loop, before measuring silencing using the FISH technique described above.

Longer loop size improved silencing, and it was found that this was dependent on better association with the DICER protein.

Introducing mismatches in the nucleotides was also trialled, as this is common in biological settings – many endogenous microRNAs have these mismatches which prevent them from binding the target gene perfectly.

What they found was that the altered shRNA had not problem binding DICER, but was inhibited in its handover to the RISC complex.

This is important, because it may be a way for cells to control the power of microRNAs, in cases where protein translation must be fine tuned.

Thanks for reading – that’s me over and out for this meeting.

Bicycle repair shack.jpg

A local bicycle repair shack in Taipei

Michael Shannon (Dylan Owen lab, KCL)