Untangling the complexity of membrane protein folding |
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| Institution: | 1. Department of Chemistry, Michigan State University, East Lansing, MI, 48824, USA;2. Wallace H. Coulter Department of Biomedical Engineering and Parker H. Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology and Emory University, Atlanta, GA, 30332, USA;3. School of Biological Sciences and Institute for Molecular Biology and Genetics, Seoul National University, Seoul, 08826, South Korea;1. The Shmunis School of Biomedicine and Cancer Research, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel;2. School of Neurobiology, Biochemistry & Biophysics, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel;1. Departments of Molecular Physiology and Biomedical Engineering, University of Virginia, Box 800886, Charlottesville, VA, 22908, USA;2. Department of Cell and Molecular Biology, Uppsala University, Box 256, Uppsala 75105, Sweden;1. RIKEN Cluster for Pioneering Research, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan;2. RIKEN Center for Biosystems Dynamics Research, 1-6-5 Minatojima-Minamimachi, Chuo-ku, Kobe, Hyogo 650-0047, Japan;3. Artificial Intelligence Center for Health and Biomedical Research, National Institutes of Biomedical Innovation, Health, and Nutrition 7-6-8, Saito-Asagi, Ibaraki, Osaka, 567-0085, Japan;4. RIKEN Center for Computational Science, 7-1-26 Minatojima-minamimachi, Chuo-ku, Kobe, Hyogo 650-0047, Japan;1. Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 7600001, Israel;2. Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot 7600001, Israel;1. Section of Biochemistry, Department of Experimental and Clinical Biomedical Sciences “Mario Serio”, University of Florence, Viale GB Morgagni 50, 50134 Florence, Italy;2. Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, United States;3. The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, United States |
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| Abstract: | Delineating the folding steps of helical-bundle membrane proteins has been a challenging task. Many questions remain unanswered, including the conformation and stability of the states populated during folding, the shape of the energy barriers between the states, and the role of lipids as a solvent in mediating the folding. Recently, theoretical frames have matured to a point that permits detailed dissection of the folding steps, and advances in experimental techniques at both single-molecule and ensemble levels enable selective modulation of specific steps for quantitative determination of the folding energy landscapes. We also discuss how lipid molecules would play an active role in shaping the folding energy landscape of membrane proteins, and how folding of multi-domain membrane proteins can be understood based on our current knowledge. We conclude this review by offering an outlook for emerging questions in the study of membrane protein folding. |
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