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Department of Chemistry

Pernilla Wittung-Stafshede

Professor of Chemistry and BioSciences

Charles W. Duncan Jr.- Welch Chair in Chemistry

CPRIT Scholar in Cancer Research

Professor, Applied Physics Graduate Program

Prof. Wittung-Stafshede's research group uses biophysical and biochemical tools to study (dys)fuctional properties of proteins and biological pathways at the molecular level. We focus on copper-binding proteins linked to cancer and misfolded proteins in neurodegenerative diseases, often with a central theme of cross-reactivity between different biomolecules.

Public Rice profile source

Average rating

3.2

14 temporary mock ratings

Difficulty

3.9

course-linked average

Courses

8

in seeded sections

Public profile

Biography

Wittung-Stafshede earned a Ph.D. in Physical Chemistry in 1996 from Chalmers University of Technology, Gothenburg, Sweden. She conducted postdoctoral research from 1997 to1998 at the California Institute of Technology in Pasadena, California. In 1999, she began her independent academic career as Assistant Professor in the Department of Chemistry at Tulane University, New Orleans, Louisiana, where she was promoted to Associate Professor with tenure in 2002. In 2004, she joined Rice University as Associate Professor with tenure in the Biosciences Department. In 2008, she returned to Sweden to become Full Professor in the Department of Chemistry at Umeå University. In 2015, she moved to Chalmers University of Technology to join the newly founded Life Sciences Department, where she also served as Head of the Chemical Biology Division for three years. In July 2025, she rejoined Rice University as Professor of Chemistry. During her academic career in the US and Sweden, she has made pioneering discoveries around the role of metals in protein folding, macromolecular crowding effects on folding reactions, as well as on mechanisms of copper-transport proteins. Her current research focuses on unraveling underlying mechanisms of devastating human diseases. Wittung-Stafshede was elected to the Royal Swedish Academy of Sciences in 2016 and to the Royal Swedish Academy of Engineering Sciences in 2020. She became an Honorary Fellow of the Royal Society of Chemistry in 2024 and was elected to the European Academy of Sciences and the Finnish Society of Sciences and Letters in 2024. She has received numerous awards and distinctions, including the Arrhenius Medal, the IUPAC Distinguished Women in Chemistry and Chemical Engineering Award, and recognition as a Fellow of the Biophysical Society. She has served on the Nobel Committee in Chemistry since 2020 and as a member of the Scientific Council for the Lindau Nobel Laureate Meetings since 2021. For more than a decade, she has contributed to the Biophysical Society in various leadership roles. Wittung-Stafshede has trained 18 doctoral students and over 25 postdoctoral researchers, many of whom have contributed to successful careers in academic and industry. In 2019, she launched and led the Gender Initiative for Excellence, a long-term initiative at Chalmers, which aimed to increase research excellence via recruitment and cultural/system changes. She is actively engaged in outreach and popular science to inspire the public, young students, and children. She has two daughters, born in 2001 and 2005.

Research areas

Chemical Biology, Inorganic Chemistry, Experimental Physical Chemistry, Chemistry of Life

Keywords

amyloid, neurodegeneration, cancer, copper homeostasis, spectroscopy, protein purification

Courses taught

APPL 800

Research And Thesis

Thesis research under the supervision of faculty. Repeatable for Credit.

Applied PhysicsNone1-15 credits
3.59.5hAjayan, Pulickel, Alabastri, Alessandro, Azhang, Behnam, Bagchi, Kushal, Baraniuk, Richard G, Biswal, Sibani, Brake, Matthew, Bulchandani, Vir, Chan, Anthony, Chen, Songtao, Dai, Pengcheng, Grande-Allen, K. Jane, Gustavsson, Anna-Karin, Halas, Naomi, Han, Yimo, Huang, Shengxi, Hulet, Randy, Kampouri, Stavroula, Kemere, Caleb, Killian, Thomas, Kono, Junichiro, Lee, Hae Yeon, Luan, Lan, Ma, Xuedan, Marciel, Amanda, Martin, Lane, Mohite, Aditya, Morosan, Emilia, Naik, Gururaj, Natelson, Doug, Nordlander, Peter, Pagano, Guido, Patel, Ankit, Patel, Tirthak, Pu, Han, Raphael, Rob, Robinson, Jacob, Sabharwal, Ashutosh, Sempionatto Moreto, Juliane, Shah, Nishal, Shee, James, Si, Qimiao, Szablowski, Jerzy, Tang, Ming, Tkaczyk, Tomasz, Tour, James, Tringides, Christina, Veeraraghavan, Ashok, Verduzco, Rafael, Vlassakis, Julea, Wehmeyer, Geoff, Wittung Stafshede, Pernilla, Wolynes, Peter, Wong, Michael, Xie, Chong, Xie, Yonglong, Yi, Ming, Zhang, Yirui Arlene, Zhao, Yuji, Zhu, Hanyu

BIOS 310

Ind Res For Bios Undergrads

Independent research in Rice BioSciences faculty laboratories (sections 2 and above) or other Texas Medical Center laboratories (section 1). Students must have secured a research position prior to applying for BIOS 310. Students spend at least 42 hours in the laboratory for each semester hour of credit (>9h/week for 3 credits). A minimum of 3 credit hours is needed to count toward the BS in Biosciences or to replace one required 300+ level elective lab course for the BA in Biosciences (cannot replace major concentration core labs). Requires a proposal abstract, weekly reports, and a research paper (fall/spring/summer) or a poster presentation (spring/summer for advanced students). Students wishing to perform their research in an off-campus lab must apply online (biosugresearch.rice.edu) at least 3 weeks prior to the start of classes and may not register for fewer than 3 credit hours. Students taking BIOS 310 in the full summer semester must be available to do full-time research for a minimum of 6 weeks or part-time equivalent which should equal to a total of 126 hours working in the lab. It is recommended that summer students spread their hours over 8-10 weeks. Recommended Prerequisite(s): Students are strongly advised to secure research advisors and register for the class well in advance of the start of classes. Recommended Prerequisite(s): Students are strongly advised to secure research advisors and register for the class well in advance of the start of classes. Repeatable for Credit.

BiosciencesNone1-5 credits
4.06.7hAjo-Franklin, Caroline, An, Linna, Bartel, Bonnie, Bashor, Caleb, Beason-Abmayr, Beth, Bennett, Matthew, Braam, Janet, Carson, Daniel, Catanese, Jamie, Chappell, James, de Moraes, Marcos, Dunham, Amy, Egan, Scott, Evans, Kory, Flynn, Jonathan, Gao, Yang, Glasscock, Cameron, Gustin, Michael, Hennelly, Lauren, Hilton, Isaac, Iyer, Harini, Johnson, Cassidy, Kirienko, Natasha, Kranz, Sven, Lavery, Laura, Lieberman-Aiden, Erez, Loveless, Theresa, Lu, George, Lwigale, Peter, Masiello, Carrie, Matsuda, Seiichi P., McCary, Matt, McNew, James, Miller, Thomas, Nakhleh, Luay, Nikonowicz, Edward, Novak, Joseph, Olmos, Joey, Onuchic, Jose, Rudolf, Volker, Rummel, Andrea, Segatori, Laura, Shamoo, Yousif, Siemann, Evan, Silberg, Joff, Solomon, Scott, Stewart, Charles, Tabor, Jeffrey, Tao, Yizhi, Uribe, Rosa, Wagner, Daniel, Wittung Stafshede, Pernilla, Wolynes, Peter, Xiao, Han

BIOS 401

Undergraduate Honors Research

The Biosciences Honors Research Program offers our seniors and advanced juniors the opportunity to perform a two-semester, individual research project in a research laboratory in Biosciences or an approved off-campus site and offers opportunities for students to develop their written and oral scientific communication skills. Students registering for BIOS 401 are expected to take BIOS 402 the following semester. Each semester, students are expected to average 15 hours per week in research (laboratory) and communication skills activities (scheduled through the companion seminar co-requisite). In BIOS 401, students will prepare regular progress reports, attend lab meetings, and write an end-of-semester short paper (at least 5 pages) on their work. Must register for co-requisite BIOS 411.

BiosciencesNone5 credits
3.89.8hAjo-Franklin, Caroline, An, Linna, Bartel, Bonnie, Beason-Abmayr, Beth, Bennett, Matthew, Braam, Janet, Carson, Daniel, Catanese, Jamie, Chappell, James, de Moraes, Marcos, Dunham, Amy, Egan, Scott, Evans, Kory, Gao, Yang, Gustin, Michael, Hennelly, Lauren, Kirienko, Natasha, Lavery, Laura, Lieberman-Aiden, Erez, Loveless, Theresa, Lwigale, Peter, Matsuda, Seiichi P., McCary, Matt, McNew, James, Miller, Thomas, Nakhleh, Luay, Nikonowicz, Edward, Onuchic, Jose, Rudolf, Volker, Rummel, Andrea, Segatori, Laura, Shamoo, Yousif, Siemann, Evan, Silberg, Joff, Solomon, Scott, Stewart, Charles, Tabor, Jeffrey, Tao, Yizhi, Uribe, Rosa, Wagner, Daniel, Wittung Stafshede, Pernilla, Wolynes, Peter, Xiao, Han

BIOS 546

Protein Folding And Misfolding

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: CHEM 546. Recommended Prerequisite(s): Undergraduate biochemistry (BIOS 301, CHEM 340) and physical chemistry (BIOS 352, CHEM 301/302)

BiosciencesNone1.5 credits
3.18.0hWittung Stafshede, Pernilla

BIOS 611

Research Seminar

Discussion of individual research or current topics in particular areas. Intended for students conducting research projects in the lab of the instructor. Repeatable for Credit.

BiosciencesNone1 credits
3.98.2hAjo-Franklin, Caroline, An, Linna, Bartel, Bonnie, Bashor, Caleb, Bennett, Matthew, Braam, Janet, Carson, Daniel, Chappell, James, de Moraes, Marcos, Gao, Yang, Glasscock, Cameron, Gustin, Michael, Han, Yimo, Hilton, Isaac, Iyer, Harini, Kirienko, Natasha, Lavery, Laura, Lieberman-Aiden, Erez, Loveless, Theresa, Luan, Lan, Lwigale, Peter, Matsuda, Seiichi P., McNew, James, Nikonowicz, Edward, Onuchic, Jose, Rosenberg, Susan, Sawakuchi, Gabriel, Segatori, Laura, Shamoo, Yousif, Silberg, Joff, Stewart, Charles, Tao, Yizhi, Uribe, Rosa, Wagner, Daniel, Wittung Stafshede, Pernilla, Wolynes, Peter, Xiao, Han, Zhou, Zheng

BIOS 800

Bcb Graduate Research

Biochemistry & Cell Biology graduate research. Repeatable for Credit.

BiosciencesNone1-15 credits
3.96.1hAjo-Franklin, Caroline, An, Linna, Bartel, Bonnie, Bashor, Caleb, Bennett, Matthew, Braam, Janet, Carson, Daniel, Chappell, James, de Moraes, Marcos, Gao, Yang, Glasscock, Cameron, Gustin, Michael, Han, Yimo, Hilton, Isaac, Iyer, Harini, Kirienko, Natasha, Lavery, Laura, Lieberman-Aiden, Erez, Loveless, Theresa, Luan, Lan, Lwigale, Peter, Matsuda, Seiichi P., McNew, James, Nikonowicz, Edward, Onuchic, Jose, Rosenberg, Susan, Sawakuchi, Gabriel, Segatori, Laura, Shamoo, Yousif, Silberg, Joff, Stewart, Charles, Tao, Yizhi, Uribe, Rosa, Wagner, Daniel, Wittung Stafshede, Pernilla, Wolynes, Peter, Xiao, Han, Zhou, Zheng

CHEM 546

Protein Folding And Misfolding

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)

ChemistryNone1.5 credits
3.57.4hWittung Stafshede, Pernilla

CHEM 800

Graduate Research

Repeatable for Credit.

ChemistryNone1-15 credits
3.97.7hAjayan, Pulickel, Alvarez, Pedro, Bagchi, Kushal, Ball, Zachary, Bao, Gang, Dai, Mingjie, Diehl, Michael, Gustavsson, Anna-Karin, Hafner, Jason, Halas, Naomi, Han, Yimo, Hartgerink, Jeffrey, Hernandez Sanchez, Raul, Hulet, Randy, Igoshin, Oleg, Jones, Matt, Kampouri, Stavroula, Kolomeisky, Anatoly, Kurti, Laszlo, Lou, Jun, Ma, Yuan, MacKintosh, Frederick, Marciel, Amanda, Marti-Arbona, Angel, Martin, Lane, Masiello, Carrie, Matsuda, Seiichi P., McHugh, Kevin, Mikos, Antonios, Mohite, Aditya, Morosan, Emilia, Mou, Quanbing, Nevidomskyy, Andriy, Nienhaus, Lea, Nordlander, Peter, Onuchic, Jose, Pasquali, Matteo, Renata, Hans, Sarlah, David, Scuseria, Gustavo, Shee, James, Tour, James, Wang, Haotian, Weisman, Bruce, West, Julian, Wittung Stafshede, Pernilla, Wolynes, Peter, Wong, Michael, Xiao, Han, Yakobson, Boris, Yruegas, Samantha

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