Uploaded March 2025 | Updated September 2026, 2 hours ago
Lecture by Professor Pernilla Wittung Stafshede, Chalmers University of Technology, at the Molecular Frontiers Symposium "Frontiers of New Knowledge in Science" in Hong Kong, Nov 15-17, 2024.
ABSTRACT
Proteins are the workhorses of all living organisms and thus essential for survival. Dysfunction or inactivity of specific proteins is the basis of most human diseases. Proteins are synthesized on ribosomes as long chains of amino acids. To become active, most of these chains need to adopt unique folded three-dimensional structures. All the information for folding is incorporated within the linear chain of amino acids and most proteins fold spontaneously in test tubes. We have thousands of proteins in our cells with different amino acid chains and thereby different folded shapes. Studies during the last decades have provided a lot of knowledge of individual protein folding reactions in test tubes. However, when considering protein folding in the cells of living organisms, additional aspects (such as the crowded environment, metal ion cofactors) need to be considered. After explaining the basics of protein folding and how we study it in the laboratory, I will describe some recent findings from my research group that showcase the importance of studying protein interactions when exploring both cancer and neurodegeneration mechanisms.
Lecture by Professor Pernilla Wittung Stafshede, Chalmers University of Technology, at the Molecular Frontiers Symposium "Frontiers of New Knowledge in Science" in Hong Kong, Nov 15-17, 2024.
ABSTRACT
Proteins are the workhorses of all living organisms and thus essential for survival. Dysfunction or inactivity of specific proteins is the basis of most human diseases. Proteins are synthesized on ribosomes as long chains of amino acids. To become active, most of these chains need to adopt unique folded three-dimensional structures. All the information for folding is incorporated within the linear chain of amino acids and most proteins fold spontaneously in test tubes. We have thousands of proteins in our cells with different amino acid chains and thereby different folded shapes. Studies during the last decades have provided a lot of knowledge of individual protein folding reactions in test tubes. However, when considering protein folding in the cells of living organisms, additional aspects (such as the crowded environment, metal ion cofactors) need to be considered. After explaining the basics of protein folding and how we study it in the laboratory, I will describe some recent findings from my research group that showcase the importance of studying protein interactions when exploring both cancer and neurodegeneration mechanisms.
