Applications of Single-Molecule Methods to Membrane Protein Folding Studies
| Autor: | Robert E. Jefferson, Jing Yang Wang, James U. Bowie, Duyoung Min, Karolina Corin |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Protein Folding Biochemistry & Molecular Biology Membrane lipids 1.1 Normal biological development and functioning atomic force spectroscopy Microscopy Atomic Force Microbiology Article Mass Spectrometry 03 medical and health sciences Membrane Lipids Medicinal and Biomolecular Chemistry Structural Biology Underpinning research Fluorescence Resonance Energy Transfer Animals Humans Molecular Biology Ability to work Microscopy magnetic tweezer Atomic force microscopy Chemistry forced unfolding Membrane protein folding Membrane Proteins Atomic Force Single Molecule Imaging 030104 developmental biology Förster resonance energy transfer Biochemistry Membrane protein Biophysics Protein folding fluorescence Generic health relevance Biochemistry and Cell Biology |
| Zdroj: | Journal of molecular biology, vol 430, iss 4 |
| Popis: | Protein folding is a fundamental life process with many implications throughout biology and medicine. Consequently, there have been enormous efforts to understand how proteins fold. Almost all of this effort has focused on water-soluble proteins, however, leaving membrane proteins largely wandering in the wilderness. The neglect has not occurred because membrane proteins are unimportant, but rather because they present many theoretical and technical complications. Indeed, quantitative membrane protein folding studies are generally restricted to a handful of well-behaved proteins. Single-molecule methods may greatly alter this picture, however, because the ability to work at or near infinite dilution removes aggregation problems, one of the main technical challenges of membrane protein folding studies. |
| Databáze: | OpenAIRE |
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