CHEMISTRY 491: Special Topics in Biochemistry Protein Folding ...

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remains a challenging problem in biochemistry. This course will introduce ... No required textbook. We will refer to 'Biochemistry' by Garrett and Grisham as.
CHEMISTRY 491:

Special Topics in Biochemistry

Protein Folding, Misfolding, and Disease Term: Prerequisites: Class time: Class location: Instructor: Inst. Office: Inst. Office hours: Inst. Phone: Inst. E-mail: Course Objective:

Spring, 2009 CHEM 351 (or equivalent) 2:30 p.m. to 3:45 p.m. Mondays and Wednesdays ACD 315 S. Jayasinghe (Jay), Ph.D. Sci II, 115 Tuesdays from 1:30 p.m. to 3:00 p.m and Fridays from 12:00 noon to 1:00 p.m. or by appointment (760) 750-8075 [email protected] Elucidating the three-dimensional structure of a protein from its sequence remains a challenging problem in biochemistry. This course will introduce students to the relevant concepts of protein structure and function, protein folding (including thermodynamics and kinetics of protein folding, protein folding in vivo), and diseases associated with protein misfolding.

Student Learning Outcomes: Upon completion of this course students should: (1). be able to describe the importance of protein structure to protein function. (2). be able to identify representative classes of proteins, and be able to describe how structure facilitates function. (3). be able to describe the basic concepts relating to the kinetics and thermodynamics of protein folding. (4). be able to describe the impact of protein misfolding on human disease and be familiar with the current research on protein misfolding. Textbook:

No required textbook. We will refer to ‘Biochemistry’ by Garrett and Grisham as the need arises (especially in the introductory/review sections).

Readings:

Course discussion will focus on relevant articles from the literature and on relevant chapters from ‘Biochemistry’ by Garrett and Grisham.

Topics : Dates are subject to change. Date

Topic

1/21/091/28/09

Introduction to Protein Structure: mainly review (primary, secondary, tertiary, quaternary structure, weak forces). Domains in proteins. Introduction to Visual Molecular Dynamics (VMD). Structure-function relationships in representative globular proteins

1/29/092/4/09

Myoglobin and hemoglobin.

2/4/092/11/09

Immunoglobulins.

2/11/092/18/09

G-proteins.

2/23/09

Guest Lecture. Dr. Barry Grant – Cytoskeletal motor proteins and motors in human disease. Structure-function relationships in representative membrane proteins

2/25/093/4/05

Bacteriorhodopsin and Rhodopsin.

3/4/093/11/09

Aquaporin.

3/11/093/18/09

KcsA – potassium channel. Protein Folding

3/16/09

Guest Lecture - Paul Whitford (Ph.D. candidate) – Functional Transitions in Proteins.

3/23/09

Guest Lecture – Dr. Joanna Sulkowska – Kinetics and thermodynamics of protein folding (concentrating on knotted proteins).

3/25/09

Guest Lecture – Dr. Joseph Hegler – Localizing frustration: consequences on binding, dynamics, and evolution.

4/6/09

Guest Lecture – Dr. Alex Shug – Computational methods in protein structure prediction.

4/8/094/15/09

In vivo protein folding (the proteasome).

4/15/094/22/09

Membrane protein folding – The translocon. Predicting transmembrane segments from sequence (hydropathy plots). Protein Misfolding and Disease

4/22/094/29/09

Aβ and Alzheimer’s disease Islet Amyloid Polypeptide (IAPP) and type II diabetes α-synuclein and Parkinson’s disease Polyglutamine and Huntington’s disease Prions

4/29/095/4/09

Influence of lipid membrane on protein misfolding.

LIterature presentations: Students will lead class discussion on a selected proteins’ structure-function relationship. Students will be responsible for reading the primary literature, summarizing the information, and presenting this information to the class. Assignments:

Students will complete a series of take home assignments. These assignments are designed to complement and extend in-class discussion and lectures. Assignments contain VMD based molecular modeling exercises, as well as, questions that will require short but well researched, and well formulated, essay type answers.

Final (exam) Project: The final project will be similar to the other take home assignments we will complete in class. Questions on the final project are comprehensive and will allow you to demonstrate your knowledge on the concepts we discussed throughout the semester. The final project is due no later than Friday May15th 2009. Reports received after this date will not be graded. Grading (points):

Attendance, class participation Literature presentations Assignments Final exam and project

50 50 150 50

Writing Requirement: The University Writing Requirement will be satisfied upon successful completion of the projects and the final project. Students with Disabilities: Students with disabilities who require accommodation must be approved by the Office of Disabled Student Services (DSS). Please contact this office as soon as possible and should meet with the instructor during office hours (or at some other mutually agreeable time). The DSS office is located in Craven hall 5205. Their telephone number is (760) 750-4905 or TTY (760) 750-4909. Academic Honesty:

All students are expected to maintain academic honesty. Students are encouraged to work in groups to complete class assignments. However, all submitted work must be your own and must be written in your own words. All students should be familiar with the university policies and procedures concerning academic honesty as detailed in the university catalog. An online version of these polices and procedures can also be found at: http://lynx.csusm.edu/policies/procedure_online.asp?ID=187