Matthias Rief

Prof. Dr. Matthias Rief holds the Chair of Biophysics at the Technical University of Munich within the Department of Bioscience at the TUM School of Natural Sciences. His research group focuses on studying protein function and folding at the single molecule level, investigating phenomena such as molecular motor motility in optical traps and protein folding/unfolding processes.

His research interests center on molecular biophysics with specific focus on protein mechanics and single-molecule analysis. The Rief Group examines how polypeptide strands fold into functional three-dimensional structures without external assistance, employing techniques like optical trapping and single-molecule force spectroscopy to understand protein behavior at the most fundamental level.

Prof. Rief's publication record shows significant contributions to understanding protein mechanics, particularly with his pioneering work on titin and other structural proteins. His research has established important methodologies for studying single-molecule protein behavior and has provided insights into fundamental biophysical principles governing protein structure and function.

• Nanoscience Prize (2003)
• Heinz Maier-Leibnitz Prize of the German Research Foundation (2000)
• Annual Prize of the German Society for Biophysics (1999)
• Doctoral Prize of the Ludwig Maximilian University of Munich (1999)

Prof. Rief teaches multiple courses including Biophysik-Winterschule, Experimentalphysik 2 für Biochemiker, Journal-Club molekulare Biophysik, and various seminars on molecular biophysics. His laboratory, the Rief Group, continues to advance the field of single-molecule biophysics with ongoing research into protein folding mechanisms and molecular motor function.

The Rief Group operates within the Department of Bioscience at TUM, collaborating with other research groups in molecular biophysics, structural biology, and related fields. The laboratory maintains state-of-the-art equipment for single-molecule manipulation and observation, enabling cutting-edge research in protein mechanics and folding dynamics.