Course Schedule and Catalog
Course Schedule - Fall Semester 2026
Meeting location information can now be found on student schedules in ESTHER (for students) or on the Course Roster in ESTHER (for faculty and instructors).Additional information available here.
Meeting location information can now be found on student schedules in ESTHER (for students) or on the Course Roster in ESTHER (for faculty and instructors).Additional information available here.
CHEM 546 001 (CRN: 16336)
PROTEIN FOLDING AND MISFOLDING
Long Title: PRINCIPLES AND METHODS OF PROTEIN FOLDING AND MISFOLDING
Department: Chemistry
Instructor: Wittung Stafshede, Pernilla
Meeting: 5:45PM - 7:00PM TR (14-OCT-2026 - 4-DEC-2026)
Part of Term: 2nd Half of Full Term
Grade Mode: Standard Letter
Course Type: Lecture
Language of Instruction: Taught in English
Method of Instruction: Face to Face
Credit Hours: 1.5
Course Syllabus:
Course Materials: Rice Campus Store
Restrictions:
Must be enrolled in one of the following Level(s):
Graduate
Section Max Enrollment: 20
Section Enrolled: 4
Total Cross-list Max Enrollment: 40
Total Cross-list Enrolled: 4
Waitlisted: 0 (Max 198)
Current members of the waitlist have priority for available seats.
Enrollment data as of: 26-APR-2026 1:13PM
Final Exam: GR Course-Dept Schedules Exam
Description: This course provides a mechanistic exploration of the biophysical principles governing protein folding, stability, and the energy landscapes that dictate functional states. A central focus is the failure of these processes—protein misfolding—and the subsequent kinetics of amyloid aggregation, a phenomenon underlying debilitating pathologies such as Alzheimer’s and Parkinson’s diseases. We will address the added complexity of the cellular proteostasis network, including the role of molecular chaperones, metal ion homeostasis, and the emerging significance of intrinsically disordered proteins and liquid-liquid phase separation. Throughout the curriculum, we evaluate the advanced methodological toolkit—including spectroscopy, calorimetry, and microscopy—essential for characterizing proteins at the atomic and molecular scale. We also cover the chemical principles used to express, engineer, and purify proteins for subsequent experiments. Cross-list: BIOS 546. Recommended Prerequisite(s): Undergraduate biochemistry (BIOS 301, CHEM 340) and physical chemistry (BIOS 352, CHEM 301/302)