To be considered for the Collins Memorial Library Undergraduate Research Award, please complete
the questions below and submit the form electronically to Jamie Spaine (jspaine@pugetsound.edu).
Your answers should be brief (no more than 500 words per question), clear, and detailed.
We’re interested in all aspects of your learning process, so answers that detail challenges or problem
solving are encouraged. You won’t lose points for encountering obstacles, but we want to know how
you overcame them. Students will be evaluated on the degree to which they:
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Make extensive and creative use of library services, resources and collections in a variety of
formats
Clearly state their research problem and situate it within the scholarly context
Demonstrate enthusiasm, knowledge and competence in their subject area
Articulate the development of their research skills during the project
Name: Jordan Carelli
Contact Information: jcarelli@pugetsound.edu; 510-384-7815
Project Title: Quantitation of underivatized sugars in solution by cesium attachment using online LCESI-MS, with applications to kinetic studies of the putative α-1,4-glycosidase MalA from Bdellovibrio
bacteriovorus.
1. Reflectively describe your literature research process. Tell us how you used library resources or
services of any kind (from ILL to online databases to archives collections to meeting with your
liaison librarian).
Around the turn of the last calendar year I began my journeys through the literature to first find,
and then explore deeply, a new research project for the Chemistry department. As I had decided to
begin a new project with Professor John Hanson, and not adopt an existing project as is more common
practice in undergraduate scientific research, the whole of my research experience involved, and
continues to involve, heavy use of the literature. During the course of my research, I delved into the
literature behind four major topics: 1) Characterization of glycosidases (enzymes that modify sugars); 2)
Mass spectrometery of sugars; 3) Use of liquid chromatography for separation of polymeric sugars in
solution; 4) Organic synthesis of sugar. For each of these subtopics within my research, I found the
most––at least initially––useful resources are published in hard-cover books. I found hard-cover
resources are generally very thorough in their review of a topic until the publication date, generally
present topics in an ideal introductory light, and give extensive reference for further technical
information. Often I found these texts in the fourth floor our the Collins Memorial Library, or was able
to quickly acquire the texts through Summit or ILLiad.
In particular, a series of hard-copy volumes in the stacks at Collins Memorial Library entitled
Methods in Enzymology provided a great starting point for finding first references on glycosidase
characterization. Methods in Enzymology serves as a sort of standard reference of methods for studying
enzymes, and each article is followed by extensive references to other relevant studies. Other
particularly useful texts included hard-cover publications of the Journal of Chromatography, Advances in
Carbohydrate Chemistry and Biochemistry, and several comprehensive texts on the organic synthesis of
sugars. These texts always lead to relevant journal article citations, which are generally necessary to find
when practicing an experimental science, as the original articles include all the valuable experimental
details and specific results. I also searched for “point” journal articles, from which I derived many other
references, though PubMed, Google Scholar, and searches within the American Chemical Society
plethora of online-accessible journals.
Once I found a potentially useful article citation, I used the
Collins Memorial Library Journal Locator to see if I could immediately find the article. If not, I entered
the citation into ILLiad, and generally receive an electronic scan of the article within a few days, or at
most a week or two. I also found back-referencing articles (“cited by”) through Google Scholar to be an
effective method of finding newer articles that draw on those which I had already found useful. This
method of literature research is iterative and only ended when I felt that I have covered a somewhat
comprehensive historical study of a topic and that I could pursue the topic experimentally. This wasn’t
quite as daunting as it sounds, as authors generally include sufficient background in introductions to at
least understand, if not find references for, the history of a topic’s study.
2. Tell us about a challenge you faced during your literature research and how you overcame it.
The most challenging references for me to find were organic syntheses. As I was generally
seeking simple sugar derivatives that aren’t the topics of many modern research papers, online
searching within Google Scholar, or the American Chemical Society generally returned irrelevant modern
articles. Here, my research advisor John Hanson was extremely helpful in teaching me tricks to using a
fantastic online resource, SciFinder. SciFinder allows for searches based on keyword, chemical structure,
or reagents, and allowed me to find the obscure German synthesis preformed in the 1970’s that I
needed.
Furthermore, I think I initially undervalued the hardcover texts on organic synthesis available in
the Collins Library. These continually proved invaluable resources, especially for basic transformations
that aren’t the spotlight of modern research.
3. How does your research contribute to the scholarly conversation in your field? What is the
significance of your research, in layperson’s terms?
The ultimate goal of my project is to contextualize the presence of an anomalous enzyme within
the genome of the bacteria-eating-bacteria Bdellovibrio bacteriovorous. Early studies on the bacteria’s
metabolism showed that it did not utilize sugars from it’s prey––only fats, proteins, and nucleic acids.
When the bacteria’s genome was sequenced in 2005, the sequence of three genes appeared to be about
60% similar to genes in other organisms that code for sugar-metabolizing enzymes. One of these is
MalA, a putative α-1,4-glycosidase, the focus of my research. Without an obvious use for an enzyme that
metabolizes sugars, our goal, set out by Mark Martin in the Biology department, is to discover the
precise function of the enzyme so that we might begin to understand or discover a previously
misunderstood or unknown part of the bacteria’s metabolic life.
The primary focus of my summer work on the project was to establish a method for quantitating
the sugar content of a solution––this is the first step in being able to understand in what manner an
enzyme might change sugars. Traditionally, similar enzymes have been studied by analyzing the
concentration of the most simple sugar unit, glucose, by a multi-step enzymatic-chemical reaction that
allows glucose concentration to be determined. I am working to develop a highly sensitive method with
liquid chromatography coupled to mass spectrometery (LC MS) to quantitate concentrations of glucose
and polymers of glucose in solution. Variations of this technique have been used to study the glucose
concentration of a diabetic’s urine, or sugar composition of fruit juices. With an LC MS method tailored
to the detection of probable substrates and products of MalA, we will be able to precisely and
conveniently characterize its activity, which is requisite to understanding the enzyme’s function. Beyond
the immediate in-house application of this LC MS method to Bdellovibrio’s metabolism, the same
methodology should be useful for the convenient study of other sugar-associated enzymes, or analysis
of any sugar-containing solution.
I will be continuing this work as my senior thesis, and am very hopeful that I will soon have the
LC MS method working and verified for use in characterization studies. I will also continue some
preliminary organic syntheses that I began this summer to produce substrate derivatives for the
enzyme. I will assay MalA with the completed substrate derivatives for changes in activity using the LC
MS method, and begin to elucidate how the enzyme interacts with its substrate. Understanding enzymesubstrate interactions will help us place the function of the enzyme within the context of the greater
organism.