Molecular Switch between Structural Compaction and Thermodynamic Stability by the Xxx-Pro Interface in Transmembrane β-Barrels
| Autor: | Anjana George, Bharat Ramasubramanian Iyer, Roshika Ravi, Swadha Gupta, Henna Noordeen, Meera Daulatrao Pawar, Radhakrishnan Mahalakshmi |
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| Rok vydání: | 2019 |
| Předmět: |
Molecular switch
Models Molecular Protein Folding Proline Chemistry Escherichia coli Proteins Lipid Bilayers Compaction Membrane Proteins Biochemistry Transmembrane protein Protein Structure Secondary Biophysics Escherichia coli Thermodynamics Chemical stability Amino Acid Sequence Lipid bilayer Bacterial outer membrane Acyltransferases |
| Zdroj: | Biochemistry. 59(3) |
| ISSN: | 1520-4995 |
| Popis: | Transmembrane β-barrel scaffolds found in outer membrane proteins are formed and stabilized by a defined pattern of interstrand intraprotein H-bonds, in hydrophobic lipid bilayers. Introducing the conformationally constrained proline in β-barrels can cause significant destabilization of these structural regions that require H-bonding, with proline additionally acting as a secondary structure breaker. Membrane protein β-barrels are therefore expected to show poor tolerance to the presence of a transmembrane proline. Here, we assign a thermodynamic measure for the extent to which a single proline can be tolerated at the C-terminal interface of the model transmembrane β-barrel PagP. We find that proline drastically destabilizes PagP by 7.0 kcal mol |
| Databáze: | OpenAIRE |
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