Relevant Thesis-Based Degree Programs
1. genetic and chemical modification to engineer functional amyloid
2. examine misfolding and aggregation of prion proteins
3. conversion of plant proteins into nanofibrils for use in foods
4. mechanisms of biofilm-associated amyloid fibril formation
Complete these steps before you reach out to a faculty member!
- Familiarize yourself with program requirements. You want to learn as much as possible from the information available to you before you reach out to a faculty member. Be sure to visit the graduate degree program listing and program-specific websites.
- Check whether the program requires you to seek commitment from a supervisor prior to submitting an application. For some programs this is an essential step while others match successful applicants with faculty members within the first year of study. This is either indicated in the program profile under "Admission Information & Requirements" - "Prepare Application" - "Supervision" or on the program website.
- Identify specific faculty members who are conducting research in your specific area of interest.
- Establish that your research interests align with the faculty member’s research interests.
- Read up on the faculty members in the program and the research being conducted in the department.
- Familiarize yourself with their work, read their recent publications and past theses/dissertations that they supervised. Be certain that their research is indeed what you are hoping to study.
- Compose an error-free and grammatically correct email addressed to your specifically targeted faculty member, and remember to use their correct titles.
- Do not send non-specific, mass emails to everyone in the department hoping for a match.
- Address the faculty members by name. Your contact should be genuine rather than generic.
- Include a brief outline of your academic background, why you are interested in working with the faculty member, and what experience you could bring to the department. The supervision enquiry form guides you with targeted questions. Ensure to craft compelling answers to these questions.
- Highlight your achievements and why you are a top student. Faculty members receive dozens of requests from prospective students and you may have less than 30 seconds to pique someone’s interest.
- Demonstrate that you are familiar with their research:
- Convey the specific ways you are a good fit for the program.
- Convey the specific ways the program/lab/faculty member is a good fit for the research you are interested in/already conducting.
- Be enthusiastic, but don’t overdo it.
G+PS regularly provides virtual sessions that focus on admission requirements and procedures and tips how to improve your application.
ADVICE AND INSIGHTS FROM UBC FACULTY ON REACHING OUT TO SUPERVISORS
These videos contain some general advice from faculty across UBC on finding and reaching out to a potential thesis supervisor.
Graduate Student Supervision
Master's Student Supervision
Theses completed in 2010 or later are listed below. Please note that there is a 6-12 month delay to add the latest theses.
Food protein nanofibrils may have improved functionalities in food applications owing to their highly ordered structures and extreme aspect ratios. Protein fibrillization is typically inducible at high temperature and low pH, where proteins are hydrolyzed and self-assemble into fibrils spontaneously. This process may be accelerated by seeding with fragments of pre-formed fibrils. As plant proteins are becoming more prevalent as environmentally sustainable and healthy alternatives to animal proteins, more research has begun to focus on legume protein fibrillization. Lentils are a major Canadian pulse crop with high protein content, but little is known about lentil protein fibrillization. The objectives of this project were to evaluate (1) the effects of protein extraction conditions (acidic vs. alkaline pH), (2) seeding with pre-formed fibrils on lentil protein fibrillization, and (3) the gelation of lentil protein fibrils. Lentil proteins extracted at either pH 8.2 or pH 3.5 with salt were incubated at 80 °C, pH 2, with stirring, to form fibrils. The protein composition and hydrolysis pattern during fibrillization and the fibrillization kinetics of the two protein extracts were found to be similar. However, transmission electron microscopy revealed apparent morphological differences—fibrils made from alkaline extract were more heterogeneous, curly, and tangled, whereas fibrils made from acidic extract were more uniform, long, and straight. Further analyses with UV-vis spectroscopy, the Fast Blue BB assay, and LC-MS indicated the presence of protein-phenolic interactions in the alkaline extract, which likely affected fibrillization. The acidic extracts were used for further studies of fibrillization. The lag time, growth rate, conversion yield, and fibril morphology were evaluated for seeded and unseeded fibrillization. Seeding with 3% w/w seeds significantly decreased the lag time (p
The full abstract for this thesis is available in the body of the thesis, and will be available when the embargo expires.
Amyloid fibrils are gaining attention as novel food ingredients and nanomaterials, due to their unique structural and chemical properties, and functionality as stabilizers and gelling agents. Amyloid fibrils are long, thin, unbranched protein aggregates that are important in medicine, biology and nanotechnology. Many proteins, including food proteins (e.g., from milk, eggs, and legumes), can be converted into amyloid fibrils under the proper conditions, most commonly by heating at low pH. Most of the research on nanofibrils has dealt with animal proteins, so a fundamental understanding of the self-assembly, structure, and functionality of nanofibrils derived from plant proteins is lacking. Plant protein is considered a sustainable source of protein. However, the functional properties of plant proteins, such as foaming, gelling, and emulsification, are generally inferior to that of animal proteins. Consequently, one method to improve the functionality of plant proteins is to produce nanofibrils, which are promising materials.The goal of this research was to relate nanofibril structure and functionality by comparing nanofibrils made from various legume proteins. Nanofibrils were formed from peanut, lentil, pea, and mung bean during incubation at pH 2 and 85 °C. The results showed that protein extracts from peanut, mung bean, pea, and lentil formed nanofibrils, which were detected using thioflavin T and transmission electron microscopy (TEM). SDS-PAGE revealed that extensive protein hydrolysis occurred during the onset of fibril formation, indicating the significance of hydrolysis to fibrillation under these conditions. Using TEM, fibrils from different legumes showed morphological variability with differences in length, width, and flexibility. This research revealed that peanut, lentil, and mung bean fibrils were most soluble at pH 2 and least soluble at isoelectric point (pI) pH. Also, the fibrils showed smaller particle size at pH 2 to that of pH 7 which is consistent with the solubility result. The presence of the fibrils results in an increase in viscosity compared to the unheated samples. The findings showed that a better understanding of legume fibrils is needed to increase their usage as functional materials in food systems, and that this would probably extend theoretical knowledge of the structure-function relationship between plant-based fibrils.