CHEMISTRY 553 Enzymology
Intersession 2000
Joseph H. Dreisbach
304 St. Thomas Hall
Office 570-941-7560
Email: dreisbachj1@scranton.edu

OFFICE HOURS: Office hours are scheduled for the hour before each class meeting, and also by appointment.

THE COURSE: The word enzymology literally means "study of enzymes". An enzyme is a protein catalyst and, although other biological molecules with catalytic activity have been identified, enzymes are the most important and abundant biological catalysts. In this course we will focus on studying the structure and function of this fascinating class of biomolecules.

CHEM 553 is an advanced graduate course. As such, it will be presented with the assumption that every student is comfortable with fundamental concepts of biochemical structure-function relationships, chemical kinetics and thermodynamics.

A tentative syllabus is provided in this document. The course starts with a review of the basic structure and chemistry of proteins and it quickly moves to mechanism and kinetics of biocatalysis. Many enzymes play key regulatory roles in metabolism and this feature is also a major topic for discussion. The course continues with some aspects of applied enzymology and concludes with a few case examples of well-characterized enzymes.

Objectives:

Students will demonstrate an ability to use fundamental and advanced concepts to solve biochemical problems dealing with enzyme structure, kinetics and mechanism.

Students will apply utilize concepts to develop a library-research paper on a case-example of an enxyme. The paper will include a host of topics covered in the classroom.

Students will utilize their knowledge of enzymology to present a focused seminar, covering specific topics from their library-research papers, to their peers and the instructor.

Students will demonstrate their understanding of concepts by directing questions to presenters and engaging in focused conversation about general and specific topics.

TEXTBOOK: Fersht, Alan. Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding. W.H. Freeman and Company, 1999. This is the primary text for the course. Other references will be made available from the reserve desk in the Weinberg Memorial Library. A basic biochemistry textbook, such as Voet and Voet, will be a valuable resource.

EVALUATION: Evaluation is performed using a variety of factors including performance on written examinations, quality of the library-research paper, effectiveness of the seminar presentation, and participation in the seminar. The assignments, point values, and due dates are provided below.

Midterm examination (January 20, 2000 tentative) 100 points
Final examination (January 27, 2000 tentative) 100 points
Research papers (due January 27, 2000 tentative) 100 points
Presentation (January 24-26, 2000 tentative) 50 points
Participation in the seminar 50 points

Scores from the examination, the independent study projects and participation will used to calculate an overall score. Final grades are determined using a distribution process but a score of 90% or greatere is guaranteed an "A"; 89-80, a "B"; and 79-70, a "C".

PROBLEM SETS: A number of problem sets will be distributed. Answers are available for examination.

MISSED WORK AND EXAMINATION POLICY: Attendance at every meeting is expected. Attendance at every examination and presentation is required. No make-up examinations are available. Solutions, if any are possible, for missed work situations, will be developed on a case-by-case basis.

POLICIES FOR CLASS CANCELLATION, MAKE-UP EXAMINATIONS AND DEADLINES. There is a possibility, indeed a history, of classes being cancelled due to inclement weather. We will adhere to the graduate school policies regarding class cancellation. Should class be cancelled, you will receive an email message from the instructor about how the evening will be recovered. You should contact the instructor, by email or telephone, if you have questions.

DATE TOPIC REFERENCE

Jan 3     Introduction to the course
            General aspects of enzymes
            Chemical nature of proteins Fersht Chapter 1

Jan 4    Conformation properties of proteins Fersht Chapter 1
            Proteins in solution

Jan 5    Isolation and purification of enzymes

Jan 6    Chemical catalysis Fersht Chapter 2

Jan 10  Enzyme kinetics Fersht Chapter 3

Jan 11  Enzyme kinetics (continued)
            Stereochemistry of enzyme reactions Fersht Chapter 8

Jan 12 Regulation of enzyme reactions Fersht Chapter 10
           Enzyme-substrate complementarity/ Fersht Chapter 11
           Binding energy in catalysis

Jan 13 Applied enzymology Fersht Chapter 15
           Case examples of enzymes

Jan 20 Mid-term examination

Jan 24-26 Presentations

Jan 27 Final examination
 

Weinberg Memorial Library Reserve List

Course: CHEMISTRY 553
Session: Intersession 2000
Instructor: JHDreisbach (x7560)

Creighton, Thomas E. Proteins: Structure and Molecular Properties, 2^nd Edition. W.H. Freeman and Company, NY. 1993.
Cunningham, E.C., Biochemistry: Mechanisms of Metabolism. McGraw-Hill, Inc. NY, 1978.
Dixon, M. and E.C. Webb. The Enzymes. Academic Press, NY, 1979.
Palmer, T. Understanding Enzymes. Ellis Horwood, Ltd. Chichester, England, 1981.
Scopes, R. Protein Purification: Principles and Practice, Springer-Verlag, NY, 1982.
Suckling, C. (Editor). Enzyme Chemistry: Impact and Applications. Chapman and Hall, London, 1984.