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Serum albumin as a model protein in designing an undergraduate laboratory course in biochemistry
Author(s) -
BROWNING SARAH E,
ODUNUGA ODUTAYO O
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.617.5
Subject(s) - circular dichroism , albumin , protein chemistry , chemistry , biochemistry , biophysics , computational biology , biology
A previous work on the design of an undergraduate laboratory course in biochemistry using serum albumin as model protein, presented at the EB 2017 conference was widely accepted. Based on comments and suggestions from faculty colleagues, we are extending the project. Extensions to the course include using fluorescence spectroscopy to monitor and determine the kinetic parameters of chemically induced unfolding of serum albumin. Serum albumin has desirable properties that make the protein a suitable model for the laboratory course design. The protein is highly abundant in blood plasma or serum; it is very soluble and stable in a wide range of buffer, pH and salt conditions. The structure of albumin makes it an ideal candidate for students to study protein structure‐function relationship using spectroscopic methods such as fluorescence, circular dichroism, infrared and UV‐Visible spectroscopies. Of particular note is the robustness of the course in terms of cost‐effectiveness, skill‐sets and pedagogical aims. All the data presented herein were generated and analyzed by students under the guidance of the professor. This is a classic example of using faculty research as a teaching tool. Support or Funding Information Welch Foundation Grant # AN‐0008 This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .