Our laboratory is associated with several graduate education and research programs leading to doctoral degrees in the biomolecular and biochemical sciences. We are part of the Division of Basic Sciences at the Fred Hutchinson Cancer Research Center, which jointly administrates the Graduate Program in Molecular and Cellular Biology (MCB) with the University of Washington. Additionally, our laboratory (and four others at the Hutchinson Center) are members of the Graduate Program in Biomolecular Structure and Design, which is a relatively new program administrated by the University of Washington and supported by the Hutchinson Center. Dr. Stoddard is also an affiliate faculty member of the Department of Biochemistry at the University of Washington. For more information on these graduate programs, proceed to the pages shown below.
Along with Roland Strong, Dr. Stoddard teaches and adminsters a graduate level course on Protein Structure-Function studies, intended for any interested students in the molecular and cellular life sciences. The course is co-listed as ConJoint 544/MCB544. It is taught at the Fred Hutchinson Cancer Research Center on tuesday and thursday afternoons. The course is taught the first five weeks of each winter quarter. Strong teaches in even years (2014, 2016, 2018....) while Stoddard teaches in odd years (2015, 2017, 2019...).
The following link (CLICK HERE), or Click on 'View Syllabus' below) will take you to the detailed course description, including the topics and readings for each session, for Stoddard's version of this class (next offered in Weeks 1 to 5 of winter quarter, January to early February 2019).
(Taught by Stoddard every other year in odd years; next available winter quarter weeks 1 to 5 in 2019).
Meets Tues/Thurs 3:15 to 4:45 at FHCRC rooms B1-072/074. 1.5 credits.
Survey level core course primarily for first year graduate students.
While life may have arisen from an RNA-centric origin, and many of the fundamental processes comprising the flow of genetic information are governed by nucleic acids, proteins have evolved to carry out many of the core biochemical and biophysical processes required for life, such as generation of force and motion, creation of physical structures, transmission of information, and catalysis of biological reactions. Over the past 10 years, the development and use of proteins as therapeutic agents has increased dramatically, an advance that can be attributed to the enormous number of protein structures and mechanisms that have been elucidated over the past 40+ years, and the especially recent development of powerful methods for protein engineering.
This course will provide a graduate-level survey of many of the fundamental properties of proteins that govern their folding, structures and function, and at the same time will introduce students to some of the most commonly used tools (and best practices) for modeling, analyzing and modifying protein structures and properties. After devoting the first week's sessions to an introduction, refresher and enhancement of our understanding of basic structural and dynamic features of proteins, the remaining four weeks will provide a detailed examination of how protein chemistry and structure/function analyses are employed for one particular area of biotechnology and biomedicine: targeted gene modification and genome engineering.
The course will assume knowledge at the level of an advanced undergraduate biochemistry course, and will be heavily skewed towards the use of structural information to understand the physical basis of protein behavior. Emphasis will be placed upon the use and visualization of protein structural models as an essential component of fully appreciating protein behavior and function. Background and understanding in the areas we will discuss at the level of Stryer, Biochemistry or Alberts, Molecular Biology of the Cell will be assumed.