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The A&S Graduate Student Independent Study/Research form can be found here: This form should be completed by the student and instructor and then e-mailed to the Biology Director of Graduate Studies before the beginning of the appropriate semester.

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Download Biology Notes Form 1

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Listed below are links to various forms, which you might find useful. Some forms are fillable PDFs: please download the form, fill it out electronically in Adobe if possible, save, and send by email.

The easiest way to take notes using the Cornell method is to use a simple piece of lined notebook paper. The notebook paper is divided into three sections: Cues or Questions, Details, and Summary. In the first column, students can write essential questions from the lecture or vocabulary words to define. In the details column, elaborating notes are written that pertain to the cues/questions. The final section, summary, provides a generalized explanation of the content on the page. Students can also add a title at the top to describe the content of the page. Images, doodles, and graphs are also helpful additions that can be included in the details column.

Although the Cornell Method may seem rigid, there are actually a lot of ways for students to individualize the pages for their own needs. Using color helps students remember content more quickly and allows them to clearly see important information like vocabulary words. Doodles and visual cues are also helpful in memorization. When discussing chemical reactions, anatomical structures, or processes, students can easily add these to the right side of the page.

The Biology Department cares about you and your needs. We would like to hear from you. The confidential C.A.R.E.S. (Courtesy, Accountability, Responsiveness, Efficiency & Service) Form is a document created for you to interact directly with the Biology Department Chair, who will work diligently to assist in resolving any issues with a specific class faculty, or staff. Once the form is completed and submitted, the Biology Department Chairperson will contact you directly with next steps. Please note: This is a confidential form that is sent directly to the Chairperson.

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Listed below are several commonly used forms and handouts that are available electronically or as hard copies in the Dept. of Biological Sciences and the University of Pittsburgh as indicated below. Click on the highlighted links to access electronic versions of forms.

If you need a professional school requirement options (A&P, Microbiology, and Medical Terminology) we recommend you review the options on this handout. Contact the Biological Sciences Advisors with any questions.

While most studies of biomolecular phase separation have focused on the condensed phase, relatively little is known about the dilute phase. Theory suggests that stable complexes form in the dilute phase of two-component phase-separating systems, impacting phase separation; however, these complexes have not been interrogated experimentally. We show that such complexes indeed exist, using an in vitro reconstitution system of a phase-separated organelle, the algal pyrenoid, consisting of purified proteins Rubisco and EPYC1. Applying fluorescence correlation spectroscopy (FCS) to measure diffusion coefficients, we found that complexes form in the dilute phase with or without condensates present. The majority of these complexes contain exactly one Rubisco molecule. Additionally, we developed a simple analytical model which recapitulates experimental findings and provides molecular insights into the dilute phase organization. Thus, our results demonstrate the existence of protein complexes in the dilute phase, which could play important roles in the stability, dynamics, and regulation of condensates.

We first set out to quantitatively measure EPYC1-Rubisco interactions. Interactions between EPYC1 and Rubisco had been studied using immunoprecipitation15, yeast two-hybrid21, and phase separation assays18 (Fig. 1), but key quantitative information including the dissociation constant Kd and complex composition is still lacking. Here, we used fluorescence correlation spectroscopy (FCS) to look for small EPYC1-Rubisco complexes in the dilute phase (Fig. 2).

To perform an FCS experiment, samples are placed inside a chamber with a bottom coverslip surface. In practice, we noted that EPYC1 protein has an unusually-high tendency to adsorb or nucleate on coverslip surfaces (Supplementary Fig. 2), even on surfaces receiving canonical modifications for single-molecule experiments, including polyethylene glycol (PEG), polyelectrolyte multilayer or detergent24 (Supplementary Fig. 2). EPYC1 aggregation on these surfaces interfered with accurate correlation analysis. We, therefore, developed a new protocol based on electrostatically pre-coated polyethyleneimine-graft-polyethylene glycol (PEI-g-PEG, Methods) and found it to produce a surface that completely eliminates EPYC1 aggregation while alleviating (although not completely suppressing) Rubisco adsorption (Supplementary Fig. 2, Supplementary Note 1 and Methods). We performed all the imaging and FCS experiments using this improved protocol.

To quantify the EPYC1-Rubisco interaction, we extracted the EPYC1 diffusion coefficient from our FCS data (Methods) and plotted it against Rubisco concentration (Fig. 2e). We observed a gradual decrease of the EPYC1 diffusion rate as larger amounts of Rubisco were added to the solution. Note that since FCS measures average diffusion rates, the observed decay in diffusivity presumably indicates that the percentage of bound EPYC1 increases as more Rubisco is added, until the diffusion rate saturates at a plateau. We also showed that the decrease in the diffusion coefficient was not an artifact of Rubisco aggregation or of nonspecific GFP-Rubisco interaction (Supplementary Fig. 3). Further, a Rubisco mutant, previously shown to almost completely disrupt EPYC1-Rubisco interaction and pyrenoid formation in vivo16, does not slow down the diffusion of EPYC1-GFP (Supplementary Fig. 4).

In conclusion, we found EPYC1 and Rubisco form complexes in the dilute phase in equilibrium with condensates over a broad range of Rubisco and EPYC1 concentrations. The fraction of EPYC1 in complexes depends on bulk Rubisco/EPYC1 concentration ratios. These results confirm the importance of dilute-phase complexes in shaping the overall phase diagram.

This work could also have important implications to pyrenoid biology. At cell division, much of the pyrenoid disassembles then reassembles in daughter cells11, presumably to facilitate splitting of the residual pyrenoid and/or to ensure each daughter has material to form a new pyrenoid. This disassembly implies a large increase of Rubisco in the dilute phase. It is not yet clear what mechanism underpins pyrenoid disassembly, but we envision two distinct scenarios: (i) posttranslational modifications of EPYC1 could generally weaken EPYC1-Rubisco interactions, so condensates become unstable, and complexes in the dilute phase also become less stable, or (ii) modifications of EPYC1 could favor dilute phase complexes, so that condensates fall apart because the competing dilute phase complexes become more stable. Future study is needed to distinguish between these two scenarios and more generally to investigate how post-translational modifications regulate dilute-phase complexes and the overall phase behavior of the pyrenoid.

The dilute phase boundary as shown in Fig. 4a, b yields predictions for the occupants of the dilute phase. Given the strong binding between EPYC1 and Rubisco almost all possible dimer pairs will form, and so it is simple to infer the amount of free EPYC1 in the dilute phase. Specifically, the fraction of EPYC1 as monomers is given by the excess relative EPYC1 concentration to Rubisco concentration divided by the total EPYC1 concentration, all evaluated at the dilute-phase boundary. From this detailed information, predictions for the EPYC1 diffusion constant can be made by assuming that the diffusion constant is the average over the EPYC1 dilute-phase complexes. Specifically, the diffusion constant is the fraction of EPYC1 as monomers multiplied by the EPYC1 monomer diffusion constant plus the fraction of EPYC1 as dimers multiplied by the dimer diffusion constant. From Fig. 3d, the diffusion of EPYC1 as monomers is ~62 tag_hash_118m2/s and of EPYC1 as EPYC1-Rubisco heterodimers is ~42 tag_hash_119m2/s.

G.H., M.C.J., N.S.W., and Q.W. designed the study. G.H. performed experiments. T.G., J.Z., and N.S.W. developed the theoretical model. H.W. constructed the FCS apparatus. All authors contributed to interpreting results and preparing the manuscript.

The Biology B.A. program also has a solid foundation in biology, but allows more flexibility in course selection by removing some of the chemistry and quantitative requirements that characterize the B.S. program. Thus, students in the B.A. program can either add more depth and focus around a sub-discipline or have more breadth, either within the biology curriculum or by taking advantage of the B.A. elective options. Many students use this flexibility to allow them to either double major or explore other subjects of interest outside of the Biology Department. ff782bc1db